KIScKinesin motor, catalytic domain. ATPase.
|SMART accession number:||SM00129|
|Description:||Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.|
|Interpro abstract (IPR001752):|
Kinesin [(PUBMED:8542443), (PUBMED:2142876), (PUBMED:14732151)] is a microtubule-associated force-producing protein that may play a role in organelle transport. The kinesin motor activity is directed toward the microtubule's plus end. Kinesin is an oligomeric complex composed of two heavy chains and two light chains. The maintenance of the quaternary structure does not require interchain disulphide bonds.
The heavy chain is composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it is known to hydrolyse ATP, to bind and move on microtubules), a central alpha-helical coiled coil domain that mediates the heavy chain dimerisation; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.
The kinesin motor domain is located in the N-terminal part of most of the above proteins, with the exception of KAR3, klpA, and ncd where it is located in the C-terminal section.
The kinesin motor domain contains about 330 amino acids. An ATP-binding motif of type A is found near position 80 to 90, the C-terminal half of the domain is involved in microtubule-binding.
|GO process:||microtubule-based movement (GO:0007018)|
|GO function:||microtubule binding (GO:0008017), microtubule motor activity (GO:0003777), ATP binding (GO:0005524)|
Click on the following links for more information.
- Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing KISc domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with KISc domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing KISc domain in the selected taxonomic class.
- Cellular role (predicted cellular role)
Binding / catalysis: ATP-hydrolysis
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Arnal I, Wade RH
- Nucleotide-dependent conformations of the kinesin dimer interacting with microtubules.
- Structure. 1998; 6: 33-8
- Display abstract
BACKGROUND: Kinesins are crucial to eukaryotic cells. They are a superfamily of motor proteins that use ATP hydrolysis to move along microtubules. Many of these motors are heterotetramers with two heavy and two light chains. The heavy chain has a globular motor domain that interacts with microtubules and shows a similar sequence throughout the family. Compared with myosin and dynein, kinesin provides a 'simple' model for understanding molecular motors. RESULTS: Electron cryomicroscopy and three-dimensional reconstruction methods have been used to investigate microtubule-kinesin dimer complexes in different nucleotide states. Three-dimensional maps were obtained in the presence of 5'-adenylylimidodiphosphate (AMP-PNP), ADP-AIF4, ADP and apyrase. In all cases, kinesin has one attached and one free head per tubulin heterodimer. The attached heads appear very similar whereas the free heads show distinct conformations and orientations depending on their nucleotide states. CONCLUSIONS: The kinesin dimer is likely to undergo considerable conformational changes during its ATP hydrolysis cycle. In all nucleotide states, the kinesin dimer attaches to a microtubule using one motor domain with the other motor domain hanging free. Only the free domain changes conformation in the presence of different nucleotides, suggesting that it, or the region linking both motor domains to the coiled coil, is the determinant of directionality. These results give some structural clues as to how kinesin moves along microtubules and we describe possible models of kinesin movement based on currently available data.
- Block SM
- Kinesin: what gives?
- Cell. 1998; 93: 5-8
- Block SM
- Leading the procession: new insights into kinesin motors.
- J Cell Biol. 1998; 140: 1281-4
- Hirokawa N
- Kinesin and dynein superfamily proteins and the mechanism of organelle transport.
- Science. 1998; 279: 519-26
- Display abstract
Cells transport and sort proteins and lipids, after their synthesis, to various destinations at appropriate velocities in membranous organelles and protein complexes. Intracellular transport is thus fundamental to cellular morphogenesis and functioning. Microtubules serve as a rail on which motor proteins, such as kinesin and dynein superfamily proteins, convey their cargoes. This review focuses on the molecular mechanism of organelle transport in cells and describes kinesin and dynein superfamily proteins.
- Cross RA
- Molecular motors: the natural economy of kinesin.
- Curr Biol. 1997; 7: 6313-6313
- Display abstract
Kinesin is a molecular-scale walking machine. New analyses of its mechanism indicate that each step along a microtubule consumes one ATP molecule, and that the binding and cleavage of ATP precede detachment of the molecule's 'feet'. Directional walking ensues if ATP processing occurs preferentially on one foot.
- Hirokawa N
- The mechanisms of fast and slow transport in neurons: identification and characterization of the new kinesin superfamily motors.
- Curr Opin Neurobiol. 1997; 7: 605-14
- Display abstract
Progress in the identification and characterization of new carboxy-terminal motor domain type kinesin superfamily proteins (KIFs)-KIFC2, 16 new KIFs and KIF-associated protein 3 (KAP3)-has provided further insight into the molecular mechanisms of organelle transport in neurons. Developments in molecular and cellular biophysics and recombinant adenovirus infection techniques combined with transgenic mice technology have enhanced the visualization of moving forms of cytoskeletal proteins during slow transport. The results of these studies strongly support the subunit transport theory.
- Kozielski F et al.
- The crystal structure of dimeric kinesin and implications for microtubule-dependent motility.
- Cell. 1997; 91: 985-94
- Display abstract
The dimeric form of the kinesin motor and neck domain from rat brain with bound ADP has been solved by X-ray crystallography. The two heads of the dimer are connected via a coiled-coil alpha-helical interaction of their necks. They are broadly similar to one another; differences are most apparent in the head-neck junction and in a moderate reorientation of the neck helices in order to adopt to the coiled-coil conformation. The heads show a rotational symmetry (approximately 120 degrees) about an axis close to that of the coiled-coil. This arrangement is unexpected since it is not compatible with the microtubule lattice. In this arrangement, the two heads of a kinesin dimer could not have equivalent interactions with microtubules.
- Sack S et al.
- X-ray structure of motor and neck domains from rat brain kinesin.
- Biochemistry. 1997; 36: 16155-65
- Display abstract
We have determined the X-ray structure of rat kinesin head and neck domains. The folding of the core motor domain resembles that of human kinesin reported recently [Kull, F. J., et al. (1996) Nature 380, 550-554]. Novel features of the structure include the N-terminal region, folded as a beta-strand, and the C-terminal transition from the motor to the rod domain, folded as two beta-strands plus an alpha-helix. This helix is the beginning of kinesin's neck responsible for dimerization of the motor complex and for force transduction. Although the folding of the motor domain core is similar to that of a domain of myosin (an actin-dependent motor), the position and angle of kinesin's neck are very different from those of myosin's stalk, suggesting that the two motors have different mechanisms of force transduction. The N- and C-terminal ends of the core motor, thought to be responsible for the directionality of the motors [Case, R. B., et al. (1997) Cell 90, 959-966], take the form of beta-strands attached to the central beta-sheet of the structure.
- Vale RD, Fletterick RJ
- The design plan of kinesin motors.
- Annu Rev Cell Dev Biol. 1997; 13: 745-77
- Display abstract
The kinesin superfamily comprises a large and structurally diverse group of microtubule-based motor proteins that produce a variety of force-generating activities within cells. This review addresses how the structures of kinesin proteins provide clues as to their biological functions and motile properties. We discuss structural features common to all kinesin motors, as well as specialized features that enable subfamilies of related motors to carry out specialized activities. We also discuss how the kinesin motor domain uses chemical energy from ATP hydrolysis to move along microtubules.
- Kull FJ, Sablin EP, Lau R, Fletterick RJ, Vale RD
- Crystal structure of the kinesin motor domain reveals a structural similarity to myosin.
- Nature. 1996; 380: 550-5
- Display abstract
Kinesin is the founding member of a superfamily of microtubule based motor proteins that perform force-generating tasks such as organelle transport and chromosome segregation. It has two identical approximately 960-amino-acid chains containing an amino-terminal globular motor domain, a central alpha-helical region that enables dimer formation through a coiled-coil, and a carboxy-terminal tail domain that binds light chains and possibly an organelle receptor. The kinesin motor domain of approximately 340 amino acids, which can produce movement in vitro, is much smaller than that of myosin (approximately 850 amino acids) and dynein (1,000 amino acids), and is the smallest known molecular motor. Here, we report the crystal structure of the human kinesin motor domain with bound ADP determined to 1.8-A resolution by X-ray crystallography. The motor consists primarily of a single alpha/beta arrowhead-shaped domain with dimensions of 70 x 45 x 45 A. Unexpectedly, it has a striking structural similarity to the core of the catalytic domain of the actin-based motor myosin. Although kinesin and myosin have virtually no amino-acid sequence++ identity, and exhibit distinct enzymatic and motile properties, our results suggest that these two classes of mechanochemical enzymes evolved from a common ancestor and share a similar force-generating strategy.
- Moore JD, Endow SA
- Kinesin proteins: a phylum of motors for microtubule-based motility.
- Bioessays. 1996; 18: 207-19
- Display abstract
The cellular processes of transport, division and, possibly, early development all involve microtubule-based motors. Recent work shows that, unexpectedly, many of these cellular functions are carried out by different types of kinesin and kinesin-related motor proteins. The kinesin proteins are a large and rapidly growing family of microtubule-motor proteins that share a 340-amino-acid motor domain. Phylogenetic analysis of the conserved motor domains groups the kinesin proteins into a number of subfamilies, the members of which exhibit a common molecular organization and related functions. The kinesin proteins that belong to different subfamilies differ in their rates and polarity of movement along microtubules, and probably in the particles/organelles that they transport. The kinesins arose early in eukaryotic evolution and gene duplication has allowed functional specialization to occur, resulting in a surprisingly large number of different classes of these proteins adapted for intracellular transport of vesicles and organelles, and for assembly and force generation in the meiotic and mitotic spindles.
- Rayment I
- Kinesin and myosin: molecular motors with similar engines.
- Structure. 1996; 4: 501-4
- Display abstract
Structure determination of the catalytic domains of two members of the kinesin superfamily reveals that this class of molecular motor exhibits the same architecture as myosin and suggests that these microtubule- and actin-based motors arose from a common ancestor.
- Smith CA, Rayment I
- X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution.
- Biochemistry. 1996; 35: 5404-17
- Display abstract
The structure of the vanadate-trapped ADP complex of a truncated head of Dictyostelium myosin II consisting of residues Asp 2-Asn 762 has been determined by molecular replacement at 1.9 A resolution and refined to a crystallographic R-factor of 19.4%. The crystals belong to the orthorhombic space group C2221 where a = 84.50 A, b = 145.4 A, and c = 152.8 A. The conformation of the protein is similar to that of MgADP.AlF4.SlDc [Fisher, A.J., et al. (1995) Biochemistry 34, 8960-8972]. The nucleotide binding site contains a complex between MgADP and vanadate where MgADP exhibits a very similar conformation to that seen in previous complexes. The vanadate ion adopts a trigonal bipyramidal coordination. The three equatorial oxygen ligands are fairly short, average 1.7 A, relative to a single bond distance of approximately 1.8 A and are coordinated to the magnesium ion, N zeta of Lys 185, and five other protein ligands. The apical coordination to the vanadate ion is filled by a terminal oxygen on the beta-phosphate of ADP and a water molecule at bond distances of 2.1 and 2.3 A, respectively. The long length of the apical bonds suggests that the bond order is considerably less than unity. This structure confirms the earlier suggestion that vanadate is a model for the transition state of ATP hydrolysis and thus provides insight into those factors that are responsible for catalysis. In particular, it shows that the protein ligands and water structure surrounding the gamma-phosphate pocket are oriented to stabilize a water molecule in an appropriate position for in-line nucleophilic attack on the gamma-phosphorus of ATP. This structure reveals also an orientation of the COOH-terminal region beyond Thr 688 which is very different from that observed in either MgADP.BeFx.SlDc or chicken skeletal myosin subfragment 1. This is consistent with the COOH-terminal region of the molecule playing an important role in the transduction of chemical energy of hydrolysis of ATP into mechanical movement.
- Bloom GS, Endow SA
- Motor proteins 1: kinesins.
- Protein Profile. 1995; 2: 1105-71
- Display abstract
Progress regarding the kinesins is now being made at a rapid and accelerating rate. The in vivo-functions, and biophysical and enzymatic properties of kinesin itself are being explored at ever increasing levels of detail. The kinesin-related proteins now number several dozen, and although more is known about primary structure than function for most of the proteins, this trend is already reversing. For example, knowledge about the kinesin-related protein, ncd, is expanding rapidly, and more is already known about its three-dimensional structure than is known for kinesin heavy chain. This volume presents a comprehensive review of the major published works on kinesin and kinesin-related proteins. Hopefully, this manuscript will complement other recent review articles [17, 20, 25, 37, 60-62, 67, 69, 75, 85-88, 231, 233, 238, 244, 269-271, 281, 282, 292] or books [49, 227, 293] that have focused on more selective aspects of the kinesin family, or have been aimed more generally at MT motor proteins. In line with the stated purpose of the Protein Profile series, annual updates of the review on the kinesins are planned for at least the next few years.
- Fisher AJ et al.
- X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-.
- Biochemistry. 1995; 34: 8960-72
- Display abstract
The three-dimensional structures of the truncated myosin head from Dictyostelium discoideum myosin II complexed with beryllium and aluminum fluoride and magnesium ADP are reported at 2.0 and 2.6 A resolution, respectively. Crystals of the beryllium fluoride-MgADP complex belong to space group P2(1)2(1)2 with unit cell parameters of a = 105.3 A, b = 182.6 A, and c = 54.7 A, whereas the crystals of the aluminum fluoride complex belong to the orthorhombic space group C222(1) with unit cell dimensions of a = 87.9 A, b = 149.0 A, and c = 153.8 A. Chemical modification was not necessary to obtain these crystals. These structures reveal the location of the nucleotide complexes and define the amino acid residues that form the active site. The tertiary structure of the protein complexed with MgADP.BeFx is essentially identical to that observed previously in the three-dimensional model of chicken skeletal muscle myosin subfragment-1 in which no nucleotide was present. By contrast, the complex with MgADP.AlF4- exhibits significant domain movements. The structures suggest that the MgADP.BeFx complex mimics the ATP bound state and the MgADP.AlF4- complex is an analog of the transition state for hydrolysis. The domain movements observed in the MgADP.AlF4- complex indicate that myosin undergoes a conformational change during hydrolysis that is not associated with the nucleotide binding pocket but rather occurs in the COOH-terminal segment of the myosin motor domain.
- Smith CA, Rayment I
- X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7 A resolution.
- Biochemistry. 1995; 34: 8973-81
- Display abstract
The structure of the magnesium pyrophosphate complex of the truncated head of Dictyostelium myosin has been determined by molecular replacement at 2.7 A resolution and refined to a crystallographic R-factor of 16.0%. The crystals belong to the orthorhombic space group P2(1)2(1)2, where a = 105.2 A, b = 182.1 A, and c = 54.5 A. The conformation of the protein around the magnesium pyrophosphate is very similar to that seen when magnesium ADP-beryllium fluoride binds in the active site. The latter complex mimics the binding of ATP prior to hydrolysis. The pyrophosphate molecule occupies the beta- and gamma-phosphate sites, where the two phosphorus atoms are in the same positions as the beta-phosphate and the BeFx moiety of the beryllium fluoride-trapped ADP. The surrounding active site residues are almost perfectly superimposable in the two structures and the hydrogen-bonding interactions that the PPi makes with the protein are essentially identical. The similarity between the MgPPi and MgADP.BeFx complex with S1Dc suggests that the conformational change, which occurs when ATP binds to actomyosin and which reduces the affinity of myosin for actin, is caused by the binding of the gamma- and beta-phosphate groups of the nucleotide. This then implies that the role of the remainder of the substrate is to increase the binding affinity for myosin and thus to drive the equilibrium toward dissociation of myosin from actin.
- Rayment I, Holden HM
- The three-dimensional structure of a molecular motor.
- Trends Biochem Sci. 1994; 19: 129-34
- Display abstract
Myosin is one of only three proteins known to convert chemical energy into mechanical work. Although the chemical, kinetic and physiological characteristics of this protein have been studied extensively, it has been difficult to define its molecular basis of movement. With the recent X-ray structural determination of the myosin head, however, it is now possible to put forward a hypothesis on how myosin might function as a molecular motor.
- Metabolism (metabolic pathways involving proteins which contain this domain)
% proteins involved KEGG pathway ID Description 50.00 map05217 Basal cell carcinoma 50.00 map04340 Hedgehog signaling pathway
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with KISc domain which could be assigned to a KEGG orthologous group, and not all proteins containing KISc domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of KISc domains in PDB
PDB code Main view Title 1bg2 HUMAN UBIQUITOUS KINESIN MOTOR DOMAIN 1cz7 THE CRYSTAL STRUCTURE OF A MINUS-END DIRECTED MICROTUBULE MOTOR PROTEIN NCD REVEALS VARIABLE DIMER CONFORMATIONS 1f9t CRYSTAL STRUCTURES OF KINESIN MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE MOTOR ATPASE 1f9u CRYSTAL STRUCTURES OF MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE KINESIN MOTOR ATPASE 1f9v CRYSTAL STRUCTURES OF MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE KINESIN MOTOR ATPASE 1f9w CRYSTAL STRUCTURES OF MUTANTS REVEAL A SIGNALLING PATHWAY FOR ACTIVATION OF THE KINESIN MOTOR ATPASE 1goj Structure of a fast kinesin: Implications for ATPase mechanism and interactions with microtubules 1i5s CRYSTAL STRUCTURE OF THE KIF1A MOTOR DOMAIN COMPLEXED WITH MG-ADP 1i6i CRYSTAL STRUCTURE OF THE KIF1A MOTOR DOMAIN COMPLEXED WITH MG-AMPPCP 1ia0 KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM 1ii6 Crystal Structure of the Mitotic Kinesin Eg5 in Complex with Mg-ADP. 1mkj Human Kinesin Motor Domain With Docked Neck Linker 1n6m Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd 1q0b Crystal structure of the motor protein KSP in complex with ADP and monastrol 1ry6 Crystal Structure of Internal Kinesin Motor Domain 1sdm Crystal structure of kinesin-like calmodulin binding protein 1t5c Crystal structure of the motor domain of human kinetochore protein CENP-E 1v8j The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-ADP 1v8k The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-AMPPNP 1vfv Crystal Structure of the Kif1A Motor Domain Complexed With Mg-AMPPNP 1vfw Crystal Structure of the Kif1A Motor Domain Complexed With Mg-AMPPNP 1vfx Crystal Structure of the Kif1A Motor Domain Complexed With ADP-Mg-AlFx 1vfz Crystal Structure of the Kif1A Motor Domain Complexed With ADP-Mg-VO4 1x88 Human Eg5 motor domain bound to Mg-ADP and monastrol 1yrs Crystal structure of KSP in complex with inhibitor 1 2fky crystal structure of KSP in complex with inhibitor 13 2fl2 crystal structure of KSP in complex with inhibitor 19 2fl6 crystal structure of KSP in complex with inhibitor 6 2fme Crystal structure of the mitotic kinesin eg5 (ksp) in complex with mg-adp and (r)-4-(3-hydroxyphenyl)-n,n,7,8-tetramethyl-3,4-dihydroisoquinoline-2(1h)-carboxamide 2g1q crystal structure of KSP in complex with inhibitor 9h 2gm1 Crystal structure of the mitotic kinesin eg5 in complex with mg-adp and n-(3-aminopropyl)-n-((3-benzyl-5-chloro-4-oxo-3,4-dihydropyrrolo[2,1-f][1,2,4]triazin-2-yl)(cyclopropyl)methyl)-4-methylbenzamide 2gry Crystal structure of the human KIF2 motor domain in complex with ADP 2h58 Crystal structure of the KIFC3 motor domain in complex with ADP 2heh Crystal Structure of the KIF2C motor domain (CASP Target) 2hxf KIF1A head-microtubule complex structure in amppnp-form 2hxh KIF1A head-microtubule complex structure in adp-form 2ieh Crystal structure of human kinesin Eg5 in complex with (R)-mon97, a new monastrol-based inhibitor that binds as (R)-enantiomer 2kin KINESIN (MONOMERIC) FROM RATTUS NORVEGICUS 2ncd NCD (NON-CLARET DISJUNCTIONAL) DIMER FROM D. MELANOGASTER 2owm Motor domain of Neurospora crassa kinesin-3 (NcKin3) 2p4n Human Monomeric Kinesin (1BG2) and Bovine Tubulin (1JFF) Docked into the 9-Angstrom Cryo-EM Map of Nucleotide-Free Kinesin Complexed to the Microtubule 2pg2 Crystal structure of KSP in complex with ADP and thiophene containing inhibitor 15 2q2y Crystal Structure of KSP in complex with Inhibitor 1 2q2z Crystal Structure of KSP in Complex with Inhibitor 22 2rep Crystal structure of the motor domain of human kinesin family member C1 2uyi Crystal structure of KSP in complex with ADP and thiophene containing inhibitor 33 2uym Crystal structure of KSP in complex with ADP and thiophene containing inhibitor 37 2vvg Crystal Structure of the G.intestinalis Kinesin 2 GiKIN2a Motor Domain 2wbe Kinesin-5-Tubulin Complex with AMPPNP 2wog Intermediate and final states of human kinesin Eg5 in complex with S-trityl-L-cysteine 2x2r Crystal structure of human kinesin Eg5 in complex with (R)-2-amino-3-((4-chlorophenyl)diphenylmethylthio)propanoic acid 2x7c Crystal structure of human kinesin Eg5 in complex with (S)-enastron 2x7d Crystal structure of human kinesin Eg5 in complex with (S)-dimethylenastron 2x7e Crystal structure of human kinesin Eg5 in complex with (R)-fluorastrol 2xae Crystal structure of human kinesin Eg5 in complex with (R)-2-amino-3-((S)-2-methyl-1,1-diphenylbutylthio)propanoic acid 2xt3 HUMAN KIF7, A KINESIN INVOLVED IN HEDGEHOG SIGNALLING 2y5w Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer 2y65 Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer-tail complex 2zfi Crystal Structure of the Kif1A Motor Domain Before Mg Release 2zfj Crystal Structure of the Kif1A Motor Domain during Mg release: Mg-releasing Transition-1 2zfk Crystal Structure of the Kif1A Motor Domain during Mg release: Mg-releasing Transition-2 2zfl Crystal Structure of the Kif1A Motor Domain during Mg release: Mg-releasing Transition-3 2zfm Crystal Structure of the Kif1A Motor Domain After Mg Release 3b6u Crystal structure of the motor domain of human kinesin family member 3B in complex with ADP 3b6v Crystal structure of the motor domain of human kinesin family member 3C in complex with ADP 3bfn Crystal structure of the motor domain of human kinesin family member 22 3cjo Crystal structure of KSP in complex with inhibitor 30 3cnz Structural dynamics of the microtubule binding and regulatory elements in the kinesin-like calmodulin binding protein 3cob Structural Dynamics of the Microtubule binding and regulatory elements in the Kinesin-like Calmodulin binding protein 3dc4 Crystal structure of the Drosophila kinesin family member NOD in complex with ADP 3dcb Crystal structure of the Drosophila kinesin family member NOD in complex with AMPPNP 3dco Drosophila NOD (3DC4) and Bovine Tubulin (1JFF) Docked into the 11-Angstrom Cryo-EM Map of Nucleotide-Free NOD Complexed to the Microtubule 3edl Kinesin13-Microtubule Ring complex 3gbj Crystal structure of the motor domain of kinesin KIF13B bound with ADP 3h4s Structure of the complex of a mitotic kinesin with its calcium binding regulator 3hqd Human kinesin Eg5 motor domain in complex with AMPPNP and Mg2+ 3j2u Kinesin-13 KLP10A HD in complex with CS-tubulin and a microtubule 3k3b Co-crystal structure of the human kinesin Eg5 with a novel tetrahydro-beta-carboline 3k5e The structure of human kinesin-like motor protein Kif11/KSP/Eg5 in complex with ADP and enastrol. 3kar THE MOTOR DOMAIN OF KINESIN-LIKE PROTEIN KAR3, A SACCHAROMYCES CEREVISIAE KINESIN-RELATED PROTEIN 3ken Human Eg5 in complex with S-trityl-L-cysteine 3kin KINESIN (DIMERIC) FROM RATTUS NORVEGICUS 3l1c Kinesin-14 Protein Ncd, T436S Mutant 3l9h X-ray structure of mitotic kinesin-5 (KSP, KIF11, Eg5)in complex with the hexahydro-2H-pyrano[3,2-c]quinoline EMD 534085 3lre Crystal Structure Analysis of Human Kinesin-8 Motor Domain 3nwn Crystal structure of the human KIF9 motor domain in complex with ADP 3pxn Crystal structure of the Drosophila kinesin family member Kin10/NOD in complex with divalent manganese and ADP 3t0q Motor Domain Structure of the Kar3-like kinesin from Ashbya gossypii 3u06 Crystal structure of the kinesin-14 NcdG347D 3zcw Eg5 - New allosteric binding site 3zfc Crystal Structure of the Kif4 Motor Domain Complexed With Mg-AMPPNP 3zfd Crystal Structure of the Kif4 Motor Domain Complexed With Mg-AMPPNP 4a14 HUMAN KIF7, A KINESIN INVOLVED IN HEDGEHOG SIGNALLING 4a1z Eg5-1 4a28 Eg5-2 4a50 Crystal structure of human kinesin Eg5 in complex with 2-Amino-5-(3-methylphenyl)-5,5-diphenylpentanoic acid 4a51 Crystal structure of human kinesin Eg5 in complex with 1-(3-(((2-Aminoethyl)thio)diphenylmethyl)phenyl)ethanone hydrochloride 4a5y Intermediate state of human kinesin Eg5 in complex with Ispinesib 4ap0 The mitotic kinesin Eg5 in complex with Mg-ADP and ispinesib 4aqv Model of human kinesin-5 motor domain (3HQD) and mammalian tubulin heterodimer (1JFF) docked into the 9.7-angstrom cryo-EM map of microtubule-bound kinesin-5 motor domain in the AMPPPNP state. 4aqw Model of human kinesin-5 motor domain (1II6, 3HQD) and mammalian tubulin heterodimer (1JFF) docked into the 9.5-angstrom cryo-EM map of microtubule-bound kinesin-5 motor domain in the rigor state. 4as7 Eg5 complex 1 4atx Rigor kinesin motor domain with an ordered neck-linker, docked on tubulin dimer, modelled into the 8A cryo-EM map of doublecortin- microtubules decorated with kinesin 4b7b Eg5-3 4bbg Crystal structure of human kinesin Eg5 in complex with 3-(((2-Aminoethyl)sulfanyl)(3-ethylphenyl) phenylmethyl)phenol 4bn2 The crystal structure of kinesin-like protein KIF15 4bxn Eg5(WT) complex 4ck5 Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in the ADP state, based on cryo-electron microscopy experiment. 4ck6 Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in the ADP.AlFx state, based on cryo-electron microscopy experiment. 4ck7 Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in presence of adp.alfx (NECK-LINKER IN ITS DISCONNECTED CONFORMATION, based on cryo-electron microscopy experiment 4etp C-terminal motor and motor homology domain of Kar3Vik1 fused to a synthetic heterodimeric coiled coil 4frz Arabidopsis KCBP motor domain dimerized via regulatory domain 4gkr Structure of the C-terminal motor domain of Kar3 from Candida glabrata 4h1g Structure of Candida albicans Kar3 motor domain fused to maltose-binding protein 4hna Kinesin motor domain in the ADP-MG-ALFX state in complex with tubulin and a DARPIN
- Links (links to other resources describing this domain)
BLOCKS KINESIN_MOTOR_DOMAIN1 PFAM kinesin INTERPRO IPR001752