1a66: Difference between revisions
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|PDB= 1a66 |SIZE=350|CAPTION= <scene name='initialview01'>1a66</scene> | |PDB= 1a66 |SIZE=350|CAPTION= <scene name='initialview01'>1a66</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= NFATC1(416-591) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= NFATC1(416-591) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a66 OCA], [http://www.ebi.ac.uk/pdbsum/1a66 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a66 RCSB]</span> | |||
}} | }} | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:07 2008'' | ||
Revision as of 15:34, 30 March 2008
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| Ligands: | DA, DC, DG, DT | ||||||||||||
| Gene: | NFATC1(416-591) (Homo sapiens) | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES
Overview
The nuclear factor of the activated T cell (NFAT) family of transcription factors regulates cytokine gene expression by binding to the promoter/enhancer regions of antigen-responsive genes, usually in cooperation with heterologous DNA-binding partners. Here we report the solution structure of the binary complex formed between the core DNA-binding domain of human NFATC1 and the ARRE2 DNA site from the interleukin-2 promoter. The structure reveals that DNA binding induces the folding of key structural elements that are required for both sequence-specific recognition and the establishment of cooperative protein-protein contacts. The orientation of the NFAT DNA-binding domain observed in the binary NFATC1-DBD*/ DNA complex is distinct from that seen in the ternary NFATC2/AP-1/DNA complex, suggesting that the domain reorients upon formation of a cooperative transcriptional complex.
About this Structure
1A66 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the core NFATC1/DNA complex., Zhou P, Sun LJ, Dotsch V, Wagner G, Verdine GL, Cell. 1998 Mar 6;92(5):687-96. PMID:9506523
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