1a66: Difference between revisions
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==SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES== | ==SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES== | ||
<StructureSection load='1a66' size='340' side='right' caption='[[1a66]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | <StructureSection load='1a66' size='340' side='right' caption='[[1a66]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a66]] is a 3 chain structure | <table><tr><td colspan='2'>[[1a66]] is a 3 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A66 FirstGlance]. <br> | ||
</td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1a66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a66 RCSB], [http://www.ebi.ac.uk/pdbsum/1a66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a66 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1a66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a66 RCSB], [http://www.ebi.ac.uk/pdbsum/1a66 PDBsum]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a66 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Doetsch, V]] | [[Category: Doetsch, V]] | ||
[[Category: Sun, L J]] | [[Category: Sun, L J]] | ||
Revision as of 12:23, 9 August 2017
SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURESSOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES
Structural highlights
Function[NFAC1_HUMAN] Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 or IL-4 gene transcription. Also controls gene expression in embryonic cardiac cells. Could regulate not only the activation and proliferation but also the differentiation and programmed death of T-lymphocytes as well as lymphoid and non-lymphoid cells. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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