SMART: PTPc domain annotation

PTPc Protein tyrosine phosphatase, catalytic domain

SMART accession number:	SM00194
Description:
Interpro abstract (IPR000242):	Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; EC 3.1.3.48) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation and transformation [(PUBMED:9818190), (PUBMED:14625689)]. The PTP superfamily can be divided into four subfamilies [(PUBMED:12678841)]: (1) pTyr-specific phosphatases (2) dual specificity phosphatases (dTyr and dSer/dThr) (3) Cdc25 phosphatases (dTyr and/or dThr) (4) LMW (low molecular weight) phosphatases Based on their cellular localisation, PTPases are also classified as: Receptor-like, which are transmembrane receptors that contain PTPase domains [(PUBMED:16672235)] Non-receptor (intracellular) PTPases [(PUBMED:8948575)] All PTPases carry the highly conserved active site motif C(X)5R (PTP signature motif), employ a common catalytic mechanism, and share a similar core structure made of a central parallel beta-sheet with flanking alpha-helices containing a beta-loop-alpha-loop that encompasses the PTP signature motif [(PUBMED:9646865)]. Functional diversity between PTPases is endowed by regulatory domains and subunits. This entry repesents several receptor and non-receptor protein-tyrosine phosphatases. Structurally, all known receptor PTPases, are made up of a variable length extracellular domain, followed by a transmembrane region and a C-terminal catalytic cytoplasmic domain. Some of the receptor PTPases contain fibronectin type III (FN-III) repeats, immunoglobulin-like domains, MAM domains or carbonic anhydrase-like domains in their extracellular region. The cytoplasmic region generally contains two copies of the PTPase domain. The first seems to have enzymatic activity, while the second is inactive. The inactive domains of tandem phosphatases can be divided into two classes. Those which bind phosphorylated tyrosine residues may recruit multi-phosphorylated substrates for the adjacent active domains and are more conserved, while the other class have accumulated several variable amino acid substitutions and have a complete loss of tyrosine binding capability. The second class shows a release of evolutionary constraint for the sites around the catalytic centre, which emphasises a difference in function from the first group. There is a region of higher conservation common to both classes, suggesting a new regulatory centre [(PUBMED:14739250)]. PTPase domains consist of about 300 amino acids. There are two conserved cysteines, the second one has been shown to be absolutely required for activity. Furthermore, a number of conserved residues in its immediate vicinity have also been shown to be important.
GO process:	protein dephosphorylation (GO:0006470)
GO function:	protein tyrosine phosphatase activity (GO:0004725)
Family alignment:	View or

There are 3349 PTPc domains in 2657 proteins in SMART's nrdb database.

Click on the following links for more information.

Evolution (species in which this domain is found)
Click on to expand nodes. To display all proteins with a PTPc domain in a specific node, click on it.

This tree shows only several representative species. The complete taxonomic breakdown of all proteins with PTPc domain is also avaliable.

Useful shortcuts: Expand all nodes or Collapse tree
Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
Cellular role (predicted cellular role)
Cellular role: signalling
Binding / catalysis: protein tyrosine phosphatase
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Hofmann K, Bucher P, Kajava AV
- A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain.
- J Mol Biol. 1998; 282: 195-208
- Display abstract
- Mammalian Cdc25 phosphatase is responsible for the dephosphorylation of Cdc2 and other cyclin-dependent kinases at Thr14 and Tyr15, thus activating the kinase and allowing cell cycle progression. The catalytic domain of this dual-specificity phosphatase has recently been mapped to the 180 most C-terminal amino acids. Apart from a CX3R motif, which is present at the active site of all known tyrosine phosphatases, Cdc25 does not share any obvious sequence similarity with any of those enzymes. Until very recently, the Cdc25 family was the only subfamily of tyrosine phosphates for which no three-dimensional structural data were available. Using the generalized profile technique, a sensitive method for sequence database searches, we found an extended and highly significant sequence similarity between the Cdc25 catalytic domain and similarly sized regions in other proteins: the non-catalytic domain of two distinct families of MAP-kinase phosphates, the non-catalytic domain of several ubiquitin protein hydrolases, the N and C-terminal domain of rhodanese, and a large and heterogeneous groups of stress-response proteins from all phyla. The relationship of Cdc25 to the structurally well-characterized rhodanese spans the entire catalytic domain and served as template for a structural model for human Cdc25a, which is fundamentally different from previously suggested models for Cdc25 catalytic domain organization. The surface positioning of subfamily-specific conserved residues allows us to predict the sites of interaction with Cdk2, a physiological target of Cdc25a. Based on the results of this analysis, we also predict that the budding yeast arsenate resistance protein Acr2 and the ORF Ygr203w encode protein phosphatases with catalytic properties similar to that of the Cdc25 family. Recent determination of the crystal structure of the Cdc25a catalytic domain supports the validity of the model and demonstrates the power of the generalized sequence profile technique in homology-based modeling of the three-dimensional structure of a protein having a weak but significant sequence similarity with a structurally characterized protein.
- VanVactor D
- Protein tyrosine phosphatases in the developing nervous system.
- Curr Opin Cell Biol. 1998; 10: 174-81
- Display abstract
- Protein tyrosine phosphatases (PTPs) constitute a diverse family of intracellular and transmembrane proteins. Expression data and recent genetic analyses indicate that many PTPs play important roles in different aspects of nervous system development. Although PTP mechanisms are still poorly understood, current data suggest considerable complexity in these signaling pathways.
- Zhang ZY
- Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis.
- Crit Rev Biochem Mol Biol. 1998; 33: 1-52
- Display abstract
- The protein-tyrosine phosphatases (PTPases) superfamily consists of tyrosine-specific phosphatases, dual specificity phosphatases, and the low-molecular-weight phosphatases. They are modulators of signal transduction pathways that regulate numerous cell functions. Malfunction of PTPases have been linked to a number of oncogenic and metabolic disease states, and PTPases are also employed by microbes and viruses for pathogenicity. There is little sequence similarity among the three subfamilies of phosphatases. Yet, three-dimensional structural data show that they share similar conserved structural elements, namely, the phosphate-binding loop encompassing the PTPase signature motif (H/V)C(X)5R(S/T) and an essential general acid/base Asp residue on a surface loop. Biochemical experiments demonstrate that phosphatases in the PTPase superfamily utilize a common mechanism for catalysis going through a covalent thiophosphate intermediate that involves the nucleophilic Cys residue in the PTPase signature motif. The transition states for phosphoenzyme intermediate formation and hydrolysis are dissociative in nature and are similar to those of the solution phosphate monoester reactions. One strategy used by these phosphatases for transition state stabilization is to neutralize the developing negative charge in the leaving group. A conformational change that is restricted to the movement of a flexible loop occurs during the catalytic cycle of the PTPases. However, the relationship between loop dynamics and enzyme catalysis remains to be established. The nature and identity of the rate-limiting step in the PTPase catalyzed reaction requires further investigation and may be dependent on the specific experimental conditions such as temperature, pH, buffer, and substrate used. In-depth kinetic and structural analysis of a representative number of phosphatases from each group of the PTPase superfamily will most likely continue to yield insightful mechanistic information that may be applicable to the rest of the family members.
- Frearson JA, Alexander DR
- The role of phosphotyrosine phosphatases in haematopoietic cell signal transduction.
- Bioessays. 1997; 19: 417-27
- Display abstract
- Phosphotyrosine phosphatases (PTPases) are the enzymes which remove phosphate groups from protein tyrosine residues. An enormous number of phosphatases have been cloned and sequenced during the past decade, many of which are expressed in haematopoietic cells. This review focuses on the biochemistry and cell biology of three phosphatases, the transmembrane CD45 and the cytosolic SH2-domain-containing PTPases SHP-1 and SHP-2, to illustrate the diverse ways in which PTPases regulate receptor signal transduction. The involvement of these and other PTPases has been demonstrated in haematopoietic cell development, apoptosis, activation and nonresponsiveness. A common theme in the actions of many haematopoietic cell PTPases is the way in which they modulate the thresholds for receptor signalling, thereby regulating critical events in the positive and negative selection of lymphocytes. There is growing interest in haematopoietic PTPases and their associated regulatory proteins as targets for pharmaceutical intervention and in the involvement of these enzymes in human disease.
- Neel BG, Tonks NK
- Protein tyrosine phosphatases in signal transduction.
- Curr Opin Cell Biol. 1997; 9: 193-204
- Display abstract
- Protein-tyrosyl phosphorylation, regulated by protein tyrosine kinases and protein tyrosine phosphatases (PTPs), is a key cellular control mechanism. Until recently, little was known about PTPs. However, the past two years have witnessed an explosion of information about PTP structure, regulation and function. Crystal structures of several PTPs have provided insights into enzymatic mechanisms and regulation and suggested the design of 'substrate-trapping' mutants. Candidate homophilic and heterophilic ligands for transmembrane PTPs have been identified, and roles for transmembrane PTPs in regulating cell-cell interactions have been suggested. Finally, progress has been made in understanding signaling by Src homology 2 domain containing PTPs and PTPs controlling yeast osmoregulatory pathways.
- Takagi T, Moore CR, Diehn F, Buratowski S
- An RNA 5'-triphosphatase related to the protein tyrosine phosphatases.
- Cell. 1997; 89: 867-73
- Display abstract
- mRNA capping requires the sequential action of three enzymatic activities: RNA triphosphatase, guanylyl-transferase, and methyltransferase. Here we characterize a gene (CEL-1) believed to encode the C. elegans capping enzyme. CEL-1 has a C-terminal domain containing motifs found in yeast and vaccinia virus capping enzyme guanylyltransferases. The N-terminal domain of CEL-1 has RNA triphosphatase activity. Surprisingly, this domain does not resemble the vaccinia virus capping enzyme but does have significant sequence similarity to the protein tyrosine phosphatase (PTP) enzyme family. However, CEL-1 has no detectable PTP activity. The mechanism of the RNA triphosphatase is similar to that of PTPs: the active site contains a conserved nucleophilic cysteine required for activity. These results broaden the superfamily of PTP-like phosphatases to include enzymes with RNA substrates.
- Zhang ZY
- Structure, mechanism, and specificity of protein-tyrosine phosphatases.
- Curr Top Cell Regul. 1997; 35: 21-68
- Fauman EB, Saper MA
- Structure and function of the protein tyrosine phosphatases.
- Trends Biochem Sci. 1996; 21: 413-7
- Display abstract
- The tyrosine and dual-specificity phosphatases are involved in signaling, cell growth and differentiation, and the cell cycle. The enzymes share a common catalytic mechanism mediated by an active site cysteine, arginine and aspartic acid. Supplementary domains assist in targeting and substrate specificity.
- Tonks NK, Neel BG
- From form to function: signaling by protein tyrosine phosphatases.
- Cell. 1996; 87: 365-8
- Barford D, Jia Z, Tonks NK
- Protein tyrosine phosphatases take off.
- Nat Struct Biol. 1995; 2: 1043-53
- Display abstract
- Protein tyrosine phosphatases (PTPs) are a family of signal transduction enzymes that dephosphorylate phosphotyrosine containing proteins. Structural and kinetic studies provide a molecular understanding of how these enzymes regulate a wide range of intracellular processes.
- Jia Z, Barford D, Flint AJ, Tonks NK
- Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B.
- Science. 1995; 268: 1754-8
- Display abstract
- The crystal structures of a cysteine-215-->serine mutant of protein tyrosine phosphatase 1B complexed with high-affinity peptide substrates corresponding to an autophosphorylation site of the epidermal growth factor receptor were determined. Peptide binding to the protein phosphatase was accompanied by a conformational change of a surface loop that created a phosphotyrosine recognition pocket and induced a catalytically competent form of the enzyme. The phosphotyrosine side chain is buried within the period and anchors the peptide substrate to its binding site. Hydrogen bonds between peptide main-chain atoms and the protein contribute to binding affinity, and specific interactions of acidic residues of the peptide with basic residues on the surface of the enzyme confer sequence specificity.
- Zondag GC, Koningstein GM, Jiang YP, Sap J, Moolenaar WH, Gebbink MF
- Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain.
- J Biol Chem. 1995; 270: 14247-50
- Display abstract
- The receptor-like protein tyrosine phosphatases (RPTP) mu and RPTP kappa have a modular ectodomain consisting of four fibronectin type III-like repeats, a single Ig-like domain, and a newly identified N-terminal MAM domain. The function of the latter module, which comprises about 160 amino acids and is found in diverse transmembrane proteins, is not known. We previously reported that both RPTP mu and RPTP kappa can mediate homophilic cell interactions when expressed in insect cells. Here we show that despite their striking structural similarity, RPTP mu and RPTP kappa fail to interact in a heterophilic manner. To examine the role of the MAM domain in homophilic binding, we expressed a mutant RPTP mu lacking the MAM domain in insect Sf9 cells. Truncated RPTP mu is properly expressed at the cell surface but fails to promote cell-cell adhesion. Homophilic cell adhesion is fully restored in a chimeric RPTP mu molecule containing the MAM domain of RPTP kappa. However, this chimeric RPTP mu does not interact with either RPTP mu or RPTP kappa. These results indicate that the MAM domain of RPTP mu and RPTP kappa is essential for homophilic cell-cell interaction and helps determine the specificity of these interactions.
- Barford D, Flint AJ, Tonks NK
- Crystal structure of human protein tyrosine phosphatase 1B.
- Science. 1994; 263: 1397-404
- Display abstract
- Protein tyrosine phosphatases (PTPs) constitute a family of receptor-like and cytoplasmic signal transducing enzymes that catalyze the dephosphorylation of phosphotyrosine residues and are characterized by homologous catalytic domains. The crystal structure of a representative member of this family, the 37-kilodalton form (residues 1 to 321) of PTP1B, has been determined at 2.8 A resolution. The enzyme consists of a single domain with the catalytic site located at the base of a shallow cleft. The phosphate recognition site is created from a loop that is located at the amino-terminus of an alpha helix. This site is formed from an 11-residue sequence motif that is diagnostic of PTPs and the dual specificity phosphatases, and that contains the catalytically essential cysteine and arginine residues. The position of the invariant cysteine residue within the phosphate binding site is consistent with its role as a nucleophile in the catalytic reaction. The structure of PTP1B should serve as a model for other members of the PTP family and as a framework for understanding the mechanism of tyrosine dephosphorylation.
- Stuckey JA, Schubert HL, Fauman EB, Zhang ZY, Dixon JE, Saper MA
- Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate.
- Nature. 1994; 370: 571-5
- Display abstract
- Protein tyrosine phosphatases (PTPases) and kinases coregulate the critical levels of phosphorylation necessary for intracellular signalling, cell growth and differentiation. Yersinia, the causative bacteria of the bubonic plague and other enteric diseases, secrete an active PTPase, Yop51, that enters and suppresses host immune cells. Though the catalytic domain is only approximately 20% identical to human PTP1B, the Yersinia PTPase contains all of the invariant residues present in eukaryotic PTPases, including the nucleophilic Cys 403 which forms a phosphocysteine intermediate during catalysis. We present here structures of the unliganded (2.5 A resolution) and tungstate-bound (2.6 A) crystal forms which reveal that Cys 403 is positioned at the centre of a distinctive phosphate-binding loop. This loop is at the hub of several hydrogen-bond arrays that not only stabilize a bound oxyanion, but may activate Cys 403 as a reactive thiolate. Binding of tungstate triggers a conformational change that traps the oxyanion and swings Asp 356, an important catalytic residue, by approximately 6 A into the active site. The same anion-binding loop in PTPases is also found in the enzyme rhodanese.
Metabolism (metabolic pathways involving proteins which contain this domain)

Structure (3D structures containing this domain)

3D Structures of PTPc domains in PDB

PDB code	Main view	Title
1a5y		Protein tyrosine phosphatase 1b cysteinyl-phosphate intermediate
1aax		Crystal structure of protein tyrosine phosphatase 1b complexed with two bis(para-phosphophenyl)methane (bppm) molecules
1bzc		Human ptp1b catalytic domain complexed with tpi
1bzh		Cyclic peptide inhibitor of human ptp1b
1bzj		Human ptp1b complexed with tpicooh
1c83		Crystal structure of protein tyrosine phosphatase 1b complexed with 6-(oxalyl-amino)-1h-indole-5-carboxylic acid
1c84		Crystal structure of protein tyrosine phosphatase 1b complexed with 3-(oxalyl-amino)-naphthalene-2-carboxlic acid
1c85		Crystal structure of protein tyrosine phosphatase 1b complexed with 2-(oxalyl-amino)-benzoic acid
1c86		Crystal structure of protein tyrosine phosphatase 1b (r47v, d48n) complexed with 2-(oxalyl-amino-4,7-dihydro-5h- thieno[2,3-c]pyran-3-carboxylic acid
1c87		Crystal structure of protein tyrosine phosphatase 1b complexed with 2-(oxalyl-amino-4,7-dihydro-5h-thieno[2,3- c]pyran-3-carboxylic acid
1c88		Crystal structure of protein tyrosine phosphatase 1b complexed with 2-(oxalyl-amino)-4,5,6,7-tetrahydro- thieno[2,3-c]pyridine-3-carboxylic acid
1ecv		Crystal structure of protein tyrosine phosphatase 1b complexed with 5-iodo-2-(oxalyl-amino)-benzoic acid
1een		Crystal structure of protein tyrosine phosphatase 1b complexed with acetyl-d-a-d-bpa-ptyr-l-i-p-q-q-g
1eeo		Crystal structure of protein tyrosine phosphatase 1b complexed with acetyl-e-l-e-f-ptyr-m-d-y-e-nh2
1fpr		Crystal structure of the complex formed between the catalytic domain of shp-1 and an in vitro peptide substrate py469 derived from shps-1.
1g1f		Crystal structure of protein tyrosine phosphatase 1b complexed with a tri-phosphorylated peptide (rdi(ptr) etd(ptr)(ptr)rk) from the insulin receptor kinase
1g1g		Crystal structure of protein tyrosine phosphatase 1b complexed with a mono-phosphorylated peptide (etdy(ptr) rkggkgll) from the insulin receptor kinase
1g1h		Crystal structure of protein tyrosine phosphatase 1b complexed with a bis-phosphorylated peptide (etd(ptr)(ptr) rkggkgll) from the insulin receptor kinase
1g4u		Crystal structure of the salmonella tyrosine phosphatase and gtpase activating protein sptp bound to rac1
1g4w		Crystal structure of the salmonella tyrosine phosphatase and gtpase activating protein sptp
1g7f		Human ptp1b catalytic domain complexed with pnu177496
1g7g		Human ptp1b catalytic domain complexes with pnu179326
1gfy		Residue 259 is a key determinant of substrate specificity of protein-tyrosine phosphatase 1b and alpha
1gwz		Crystal structure of the catalytic domain of the protein tyrosine phosphatase shp-1
1i57		Crystal structure of apo human ptp1b (c215s) mutant
1jf7		Human ptp1b catalytic domain complexed with pnu177836
1jln		Crystal structure of the catalytic domain of protein tyrosine phosphatase ptp-sl/br7
1kak		Human tyrosine phosphatase 1b complexed with an inhibitor
1kav		Human tyrosine phosphatase 1b complexed with an inhibitor
1l8g		Crystal structure of ptp1b complexed with 7-(1,1-dioxo-1h- benzo[d]isothiazol-3-yloxymethyl)-2-(oxalyl-amino)-4,7- dihydro-5h-thieno[2,3-c]pyran-3-carboxylic acid
1l8k		T cell protein-tyrosine phosphatase structure
1lar		Crystal structure of the tandem phosphatase domains of rptp lar
1lqf		Structure of ptp1b in complex with a peptidic bisphosphonate inhibitor
1lyv		High-resolution structure of the catalytically inactive yersinia tyrosine phosphatase c403a mutant in complex with phosphate.
1nl9		Potent, selective protein tyrosine phosphatase 1b inhibitor compound 12 using a linked-fragment strategy
1nny		Potent, selective protein tyrosine phosphatase 1b inhibitor compound 23 using a linked-fragment strategy
1no6		Potent, selective protein tyrosine phosphatase 1b inhibitor compound 5 using a linked-fragment strategy
1nwe		Ptp1b r47c modified at c47 with n-[4-(2-{2-[3-(2-bromo- acetylamino)-propionylamino]-3-hydroxy-propionylamino}- ethyl)-phenyl]-oxalamic acid
1nwl		Crystal structure of the ptp1b complexed with sp7343-sp7964, a ptyr mimetic
1nz7		Potent, selective inhibitors of protein tyrosine phosphatase 1b using a second phosphotyrosine binding site, complexed with compound 19.
1oem		Ptp1b with the catalytic cysteine oxidized to a sulfenyl-amide bond
1oeo		Ptp1b with the catalytic cysteine oxidized to sulfonic acid
1oes		Oxidation state of protein tyrosine phosphatase 1b
1oet		Oxidation state of protein tyrosine phosphatase 1b
1oeu		Oxidation state of protein tyrosine phosphatase 1b
1oev		Oxidation state of protein tyrosine phosphatase 1b
1ony		Oxalyl-aryl-amino benzoic acid inhibitors of ptp1b, compound 17
1onz		Oxalyl-aryl-amino benzoic acid inhibitors of ptp1b, compound 8b
1p15		Crystal structure of the d2 domain of rptpa
1pa1		Crystal structure of the c215d mutant of protein tyrosine phosphatase 1b
1pa9		Yersinia protein-tyrosine phosphatase complexed with pncs (yop51,pasteurella x,ptpase,yop51delta162) (catalytic domain, residues 163-468) mutant with cys 235 replaced by arg (c235r)
1ph0		Non-carboxylic acid-containing inhibitor of ptp1b targeting the second phosphotyrosine site
1ptt		Crystal structure of protein tyrosine phosphatase 1b complexed with phosphotyrosine-containing tetra-peptide (ac-depyl-nh2)
1ptu		Crystal structure of protein tyrosine phosphatase 1b complexed with phosphotyrosine-containing hexa-peptide (dadepyl-nh2)
1ptv		Crystal structure of protein tyrosine phosphatase 1b complexed with phosphotyrosine
1pty		Crystal structure of protein tyrosine phosphatase 1b complexed with two phosphotyrosine molecules
1pxh		Crystal structure of protein tyrosine phosphatase 1b with potent and selective bidentate inhibitor compound 2
1pyn		Dual-site potent, selective protein tyrosine phosphatase 1b inhibitor using a linked fragment strategy and a malonate head on the first site
1q1m		A highly efficient approach to a selective and cell active ptp1b inhibitors
1q6j		The structure of phosphotyrosine phosphatase 1b in complex with compound 2
1q6m		The structure of phosphotyrosine phosphatase 1b in complex with compound 3
1q6n		The structure of phosphotyrosine phosphatase 1b in complex with compound 4
1q6p		The structure of phosphotyrosine phosphatase 1b in complex with compound 6
1q6s		The structure of phosphotyrosine phosphatase 1b in complex with compound 9
1q6t		The structure of phosphotyrosine phosphatase 1b in complex with compound 11
1qxk		Monoacid-based, cell permeable, selective inhibitors of protein tyrosine phosphatase 1b
1qz0		Crystal structure of the yersinia pestis phosphatase yoph in complex with a phosphotyrosyl mimetic-containing hexapeptide
1rpm		Human receptor protein tyrosine phosphatase mu, domain 1
1sug		1.95 a structure of apo protein tyrosine phosphatase 1b
1t48		Allosteric inhibition of protein tyrosine phosphatase 1b
1t49		Allosteric inhibition of protein tyrosine phosphatase 1b
1t4j		Allosteric inhibition of protein tyrosine phosphatase 1b
1wax		Protein tyrosine phosphatase 1b with active site inhibitor
1wch		Crystal structure of ptpl1 human tyrosine phosphatase mutated in colorectal cancer - evidence for a second phosphotyrosine substrate recognition pocket
1xbo		Ptp1b complexed with isoxazole carboxylic acid
1xxp		Yersinia yoph (residues 163-468) c403s binds phosphotyrosyl peptide at two sites
1xxv		Yersinia yoph (residues 163-468) binds phosphonodifluoromethyl-phe containing hexapeptide at two sites
1yfo		Receptor protein tyrosine phosphatase alpha, domain 1 from mouse
1ygr		Crystal structure of the tandem phosphatase domain of rptp cd45
1ygu		Crystal structure of the tandem phosphatase domains of rptp cd45 with a ptyr peptide
1ypt		Crystal structure of yersinia protein tyrosine phosphatase at 2.5 angstroms and the complex with tungstate
1ytn		Hydrolase
1yts		A ligand-induced conformational change in the yersinia protein tyrosine phosphatase
1ytw		Yersinia ptpase complexed with tungstate
1zc0		Crystal structure of human hematopoietic tyrosine phosphatase (heptp) catalytic domain
2a3k		Crystal structure of the human protein tyrosine phosphatase, ptpn7 (heptp, hematopoietic protein tyrosine phosphatase)
2a8b		Crystal structure of the catalytic domain of human tyrosine phosphatase receptor, type r
2ahs		Crystal structure of the catalytic domain of human tyrosine receptor phosphatase beta
2azr		Crystal structure of ptp1b with bicyclic thiophene inhibitor
2b07		Crystal structure of ptp1b with tricyclic thiophene inhibitor.
2b3o		Crystal structure of human tyrosine phosphatase shp-1
2b49		Crystal structure of the catalytic domain of protein tyrosine phosphatase, non-receptor type 3
2b4s		Crystal structure of a complex between ptp1b and the insulin receptor tyrosine kinase
2bgd		Structure-based design of protein tyrosine phosphatase-1b inhibitors
2bge		Structure-based design of protein tyrosine phosphatase-1b inhibitors
2bij		Crystal structure of the human protein tyrosine phosphatase ptpn5 (step, striatum enriched enriched phosphatase)
2bv5		Crystal structure of the human protein tyrosine phosphatase ptpn5 at 1.8a resolution
2bzl		Crystal structure of the human protein tyrosine phosphatase n14 at 1.65 a resolution
2c7s		Crystal structure of human protein tyrosine phosphatase kappa at 1.95a resolution
2cfv		Crystal structure of human protein tyrosine phosphatase receptor type j
2cjz		Crystal structure of the c472s mutant of human protein tyrosine phosphatase ptpn5 (step, striatum enriched phosphatase) in complex with phosphotyrosine
2cm2		Structure of protein tyrosine phosphatase 1b (p212121)
2cm3		Structure of protein tyrosine phosphatase 1b (c2)
2cm7		Structural basis for inhibition of protein tyrosine phosphatase 1b by isothiazolidinone heterocyclic phosphonate mimetics
2cm8		Structural basis for inhibition of protein tyrosine phosphatase 1b by isothiazolidinone heterocyclic phosphonate mimetics
2cma		Structural basis for inhibition of protein tyrosine phosphatase 1b by isothiazolidinone heterocyclic phosphonate mimetics
2cmb		Structural basis for inhibition of protein tyrosine phosphatase 1b by isothiazolidinone heterocyclic phosphonate mimetics
2cmc		Structural basis for inhibition of protein tyrosine phosphatase 1b by isothiazolidinone heterocyclic phosphonate mimetics
2cne		Structural insights into the design of nonpeptidic isothiazolidinone-containing inhibitors of protein tyrosine phosphatase 1b
2cnf		Structural insights into the design of nonpeptidic isothiazolidinone-containing inhibitors of protein tyrosine phosphatase 1b
2cng		Structural insights into the design of nonpeptidic isothiazolidinone-containing inhibitors of protein tyrosine phosphatase 1b
2cnh		Structural insights into the design of nonpeptidic isothiazolidinone-containing inhibitors of protein tyrosine phosphatase 1b
2cni		Structural insights into the design of nonpeptidic isothiazolidinone-containing inhibitors of protein tyrosine phosphatase 1b
2f6f		The structure of the s295f mutant of human ptp1b
2f6t		Protein tyrosine phosphatase 1b with sulfamic acid inhibitors
2f6v		Protein tyrosine phosphatase 1b with sulfamic acid inhibitors
2f6w		Protein tyrosine phosphatase 1b with sulfamic acid inhibitors
2f6y		Protein tyrosine phosphatase 1b with sulfamic acid inhibitors
2f6z		Protein tyrosine phosphatase 1b with sulfamic acid inhibitors
2f70		Protein tyrosine phosphatase 1b with sulfamic acid inhibitors
2f71		Protein tyrosine phosphatase 1b with sulfamic acid inhibitors
2fh7		Crystal structure of the phosphatase domains of human ptp sigma
2fjm		The structure of phosphotyrosine phosphatase 1b in complex with compound 2
2fjn		The structure of phosphotyrosine phosphatase 1b in complex with compound 2
2g59		Crystal structure of the catalytic domain of protein tyrosine phosphatase from homo sapiens
2gjt		Crystal structure of the human receptor phosphatase ptpro
2gp0		Heptp catalytic domain (residues 44-339), s225d mutant
2h02		Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors
2h03		Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors
2h04		Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors
2h4g		Crystal structure of ptp1b with monocyclic thiophene inhibitor
2h4k		Crystal structure of ptp1b with a monocyclic thiophene inhibitor
2h4v		Crystal structure of the human tyrosine receptor phosphatase gamma
2hb1		Crystal structure of ptp1b with monocyclic thiophene inhibitor
2hc1		Engineered catalytic domain of protein tyrosine phosphatase hptpbeta.
2hc2		Engineered protein tyrosine phosphatase beta catalytic domain
2hnp		Crystal structure of human protein tyrosine phosphatase 1b
2hnq		Crystal structure of human protein tyrosine phosphatase 1b
2hvl		Crystal structure of the heptp catalytic domain c270s mutant
2hy3		Crystal structure of the human tyrosine receptor phosphate gamma in complex with vanadate
2i1y		Crystal structure of the phosphatase domain of human ptp ia-
2i3r		Engineered catalytic domain of protein tyrosine phosphatase hptpbeta
2i3u		Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors
2i42		Crystal structure of yersinia protein tyrosine phosphatase complexed with vanadate, a transition state analogue
2i4e		Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors
2i4g		Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with a sulfamic acid (soaking experiment)
2i4h		Structural studies of protein tyrosine phosphatase beta catalytic domain co-crystallized with a sulfamic acid inhibitor
2i5x		Engineering the ptpbeta catalytic domain with improved crystallization properties
2i75		Crystal structure of human protein tyrosine phosphatase n4 (ptpn4)
2jjd		Protein tyrosine phosphatase, receptor type, e isoform
2nlk		Crystal structure of d1 and d2 catalytic domains of human protein tyrosine phosphatase gamma (d1+d2 ptprg)
2nt7		Crystal structure of ptp1b-inhibitor complex
2nta		Crystal structure of ptp1b-inhibitor complex
2nv5		Crystal structure of a c-terminal phosphatase domain of rattus norvegicus ortholog of human protein tyrosine phosphatase, receptor type, d (ptprd)
2nz6		Crystal structure of the ptprj inactivating mutant c1239s
2oc3		Crystal structure of the catalytic domain of human protein tyrosine phosphatase non-receptor type 18
2ooq		Crystal structure of the human receptor phosphatase ptprt
2p6x		Crystal structure of human tyrosine phosphatase ptpn22
2pa5		Crystal structure of human protein tyrosine phosphatase ptpn9
2pbn		Crystal structure of the human tyrosine receptor phosphate gamma
2pi7		Structure of the catalytic domain of the chick retinal neurite inhibitor-receptor protein tyrosine phosphatase cryp-2/cptpro
2qbp		Crystal structure of ptp1b-inhibitor complex
2qbq		Crystal structure of ptp1b-inhibitor complex
2qbr		Crystal structure of ptp1b-inhibitor complex
2qbs		Crystal structure of ptp1b-inhibitor complex
2qcj		Native structure of lyp
2qct		Structure of lyp with inhibitor i-c11
2qdc		Crystal structure of the heptp catalytic domain d236a mutant
2qdm		Crystal structure of the heptp catalytic domain c270s/d236a/q314a mutant
2qdp		Crystal structure of the heptp catalytic domain c270s mutant crystallized in ammonium acetate
2qep		Crystal structure of the d1 domain of ptprn2 (ia2beta)
2shp		Tyrosine phosphatase shp-2
2veu		Crystal structure of protein tyrosine phosphatase 1b in complex with an isothiazolidinone-containing inhibitor
2vev		Crystal strucutre of protein tyrosine phosphatase 1b in complex with an isothiazolidinone-containing inhibitor
2vew		Crystal strucutre of protein tyrosine phosphatase 1b in complex with an isothiazolidinone-containing inhibitor
2vex		Crystal strucutre of protein tyrosine phosphatase 1b in complex with an isothiazolidinone-containing inhibitor
2vey		Crystal strucutre of protein tyrosine phosphatase 1b in complex with an isothiazolidinone-containing inhibitor
2zmm		Crystal structure of ptp1b-inhibitor complex
2zn7		Crystal structures of ptp1b-inhibitor complexes
3b7o		Crystal structure of the human tyrosine phosphatase shp2 (ptpn11) with an accessible active site
3blt		Crystal structures of yoph complexed with pvsn and pvs, inhibitors of yoph which co-valent bind to cys of active site
3blu		Crystal structure yoph complexed with inhibitor pvs
3bm8		Crystal structure of yoph mutant d356a complexed with irreversible inhibitor pvsn
3brh		Protein tyrosine phosphatase ptpn-22 (lyp) bound to the mono-phosphorylated lck active site peptide
3cwe		Ptp1b in complex with a phosphonic acid inhibitor
3d42		Crystal structure of heptp in complex with a monophosphorylated erk2 peptide
3d44		Crystal structure of heptp in complex with a dually phosphorylated erk2 peptide mimetic
3d9c		Crystal structure ptp1b complex with aryl seleninic acid
3eax		Crystal structure ptp1b complex with small molecule compound lzp-6
3eb1		Crystal structure ptp1b complex with small molecule inhibitor lzp-25
3eu0		Crystal structure of the s-nitrosylated cys215 of ptp1b
3f99		W354f yersinia enterocolitica ptpase apo form
3f9a		W354f yersinia enterocolitica ptpase complexed with tungstate
3f9b		W354f yersinia enterocolitica ptpase complexed with divanadate
3h2x		Crystal structure of the human lymphoid tyrosine phosphatase catalytic domain

Links (links to other resources describing this domain)
PFAM Y_phosphatase
INTERPRO IPR000242
PROSITE TYR_PHOSPHATASE_PTP

PFAM	Y_phosphatase
INTERPRO	IPR000242
PROSITE	TYR_PHOSPHATASE_PTP