BRLZbasic region leucin zipper
|SMART accession number:||SM00338|
|Interpro abstract (IPR004827):||The basic-leucine zipper (bZIP) domain transcription factors [(PUBMED:7780801)] of eukaryotic are proteins that contain a basic region mediating sequence-specific DNA-binding followed by a leucine zipper region required for dimerisation.|
|GO process:||regulation of transcription, DNA-templated (GO:0006355)|
|GO function:||sequence-specific DNA binding (GO:0043565), sequence-specific DNA binding transcription factor activity (GO:0003700)|
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- Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing BRLZ domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with BRLZ domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing BRLZ domain in the selected taxonomic class.
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Muller CW, Herrmann BG
- Crystallographic structure of the T domain-DNA complex of the Brachyury transcription factor.
- Nature. 1997; 389: 884-8
- Display abstract
The mouse Brachyury (T) gene is the prototype of a growing family of so-called T-box genes which encode transcriptional regulators and have been identified in a variety of invertebrates and vertebrates, including humans. Mutations in Brachyury and other T-box genes result in drastic embryonic phenotypes, indicating that T-box gene products are essential in tissue specification, morphogenesis and organogenesis. The T-box encodes a DNA-binding domain of about 180 amino-acid residues, the T domain. Here we report the X-ray structure of the T domain from Xenopus laevis in complex with a 24-nucleotide palindromic DNA duplex. We show that the protein is bound as a dimer, interacting with the major and the minor grooves of the DNA. A new type of specific DNA contact is seen, in which a carboxy-terminal helix is deeply embedded into an enlarged minor groove without bending the DNA. Hydrophobic interactions and an unusual main-chain carbonyl contact to a guanine account for sequence-specific recognition in the minor groove by this helix. Thus the structure of this T domain complex with DNA reveals a new way in which a protein can recognize DNA.
- Hurst HC
- Transcription factors 1: bZIP proteins.
- Protein Profile. 1995; 2: 101-68
- Ellenberger T, Fass D, Arnaud M, Harrison SC
- Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer.
- Genes Dev. 1994; 8: 970-80
- Display abstract
A large group of transcription factors regulating cell growth and differentiation share a dimeric alpha-helical DNA-binding domain termed the basic region helix-loop-helix (bHLH). bHLH proteins associate as homodimers and heterodimers having distinctive DNA-binding activities and transcriptional activities that are central to the regulated differentiation of a number of tissues. Some of the bHLH residues specifying these activities have been identified, but a full understanding of their function has awaited further structural information. We report here the crystal structure of the transcription factor E47 bHLH domain bound to DNA. The bHLH of E47 is a parallel, four-helix bundle with structural features that distinguish it from the bHLH-zipper protein Max. The E47 dimer makes nonequivalent contacts to each half of the -CACCTG- binding site. Sequence discrimination at the center of the E box may result from interaction with both the DNA bases and the phosphodiester backbone.
- Anthony-Cahill SJ et al.
- Molecular characterization of helix-loop-helix peptides.
- Science. 1992; 255: 979-83
- Display abstract
A class of regulators of eukaryotic gene expression contains a conserved amino acid sequence responsible for protein oligomerization and binding to DNA. This structure consists of an arginine- and lysine-rich basic region followed by a helix-loop-helix motif, which together mediate specific binding to DNA. Peptides were prepared that span this motif in the MyoD protein; in solution, they formed alpha-helical dimers and tetramers. They bound to DNA as dimers and their alpha-helical content increased on binding. Parallel and antiparallel four-helix models of the DNA-bound dimer were constructed. Peptides containing disulfide bonds were engineered to test the correctness of the two models. A disulfide that is compatible with the parallel model promotes specific interaction with DNA, whereas a disulfide compatible with the antiparallel model abolishes specific binding. Electron paramagnetic resonance (EPR) measurements of nitroxide-labeled peptides provided intersubunit distance measurements that also supported the parallel model.
- Landschulz WH, Johnson PF, McKnight SL
- The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins.
- Science. 1988; 240: 1759-64
- Display abstract
A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein. Display of these respective amino acid sequences on an idealized alpha helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. The periodic array of at least four leucines was also noted in the sequences of the Fos and Jun transforming proteins, as well as that of the yeast gene regulatory protein, GCN4. The polypeptide segments containing these periodic arrays of leucine residues are proposed to exist in an alpha-helical conformation, and the leucine side chains extending from one alpha helix interdigitate with those displayed from a similar alpha helix of a second polypeptide, facilitating dimerization. This hypothetical structure is referred to as the "leucine zipper," and it may represent a characteristic property of a new category of DNA binding proteins.
- Metabolism (metabolic pathways involving proteins which contain this domain)
% proteins involved KEGG pathway ID Description 18.00 map05215 Prostate cancer 13.33 map04916 Melanogenesis 13.00 map04010 MAPK signaling pathway 5.67 map05210 Colorectal cancer 5.67 map04620 Toll-like receptor signaling pathway 5.67 map04662 B cell receptor signaling pathway 5.67 map04660 T cell receptor signaling pathway 5.00 map04912 GnRH signaling pathway 5.00 map04310 Wnt signaling pathway 3.00 map05060 Prion disease 2.67 map05120 Epithelial cell signaling in Helicobacter pylori infection 2.67 map04510 Focal adhesion 2.67 map04012 ErbB signaling pathway 2.67 map05211 Renal cell carcinoma 2.33 map04612 Antigen processing and presentation 2.33 map04720 Long-term potentiation 1.67 map05221 Acute myeloid leukemia 1.33 map04950 Maturity onset diabetes of the young 1.33 map04930 Type II diabetes mellitus 0.33 map04080 Neuroactive ligand-receptor interaction
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 BRLZ domain which could be assigned to a KEGG orthologous group, and not all proteins containing BRLZ 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 BRLZ domains in PDB
PDB code Main view Title 1a02 STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA 1ci6 TRANSCRIPTION FACTOR ATF4-C/EBP BETA BZIP HETERODIMER 1dgc THE X-RAY STRUCTURE OF THE GCN4-BZIP BOUND TO ATF/CREB SITE DNA SHOWS THE COMPLEX DEPENDS ON DNA FLEXIBILITY 1dh3 CRYSTAL STRUCTURE OF A CREB BZIP-CRE COMPLEX REVEALS THE BASIS FOR CREB FAIMLY SELECTIVE DIMERIZATION AND DNA BINDING 1fos TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES 1gd2 CRYSTAL STRUCTURE OF BZIP TRANSCRIPTION FACTOR PAP1 BOUND TO DNA 1gtw crystal structure of C/EBPbeta bZip homodimer bound to a DNA fragment from the tom-1A promoter 1gu4 CRYSTAL STRUCTURE OF C/EBPBETA BZIP HOMODIMER BOUND TO A HIGH AFFINITY DNA FRAGMENT 1gu5 CRYSTAL STRUCTURE OF C/EBPBETA BZIP HOMODIMER BOUND TO A DNA FRAGMENT FROM THE MIM-1 PROMOTER 1h88 CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX1 1h89 CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX2 1h8a CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX3 1hjb CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN AND C/EBPBETA BZIP HOMODIMER BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER 1io4 CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN-CBFBETA CORE DOMAIN HETERODIMER AND C/EBPBETA BZIP HOMODIMER BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER 1jnm Crystal Structure of the Jun/CRE Complex 1ld4 Placement of the Structural Proteins in Sindbis Virus 1nwq CRYSTAL STRUCTURE OF C/EBPALPHA-DNA COMPLEX 1s9k Crystal Structure of Human NFAT1 and Fos-Jun on the IL-2 ARRE1 Site 1t2k Structure Of The DNA Binding Domains Of IRF3, ATF-2 and Jun Bound To DNA 1ysa THE GCN4 BASIC REGION LEUCINE ZIPPER BINDS DNA AS A DIMER OF UNINTERRUPTED ALPHA HELICES: CRYSTAL STRUCTURE OF THE PROTEIN-DNA COMPLEX 2dgc GCN4 BASIC DOMAIN, LEUCINE ZIPPER COMPLEXED WITH ATF/CREB SITE DNA 2e42 Crystal structure of C/EBPbeta Bzip homodimer V285A mutant bound to A High Affinity DNA fragment 2e43 Crystal structure of C/EBPbeta Bzip homodimer K269A mutant bound to A High Affinity DNA fragment 2h7h Crystal structure of the JUN BZIP homodimer complexed with AP-1 DNA 2wt7 Crystal structure of the bZIP heterodimeric complex MafB:cFos bound to DNA 2wty Crystal structure of the homodimeric MafB in complex with the T-MARE binding site 3a5t Crystal structure of MafG-DNA complex 4auw CRYSTAL STRUCTURE OF THE BZIP HOMODIMERIC MAFB IN COMPLEX WITH THE C- MARE BINDING SITE 4eot Crystal structure of the MafA homodimer bound to the consensus MARE
- Links (links to other resources describing this domain)
PFAM bZIP INTERPRO IPR004827 PROSITE BZIP_BASIC