1a66: Difference between revisions

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[[Image:1a66.jpg|left|200px]]


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==SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES==
The line below this paragraph, containing "STRUCTURE_1a66", creates the "Structure Box" on the page.
<StructureSection load='1a66' size='340' side='right'caption='[[1a66]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1a66]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1A66 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a66 OCA], [https://pdbe.org/1a66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a66 RCSB], [https://www.ebi.ac.uk/pdbsum/1a66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a66 ProSAT]</span></td></tr>
{{STRUCTURE_1a66| PDB=1a66  | SCENE= }}
</table>
 
== Function ==
'''SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES'''
[https://www.uniprot.org/uniprot/NFAC1_HUMAN 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 ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/1a66_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1a66 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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==
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<ref>PMID:9506523</ref>
1A66 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A66 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://www.ncbi.nlm.nih.gov/pubmed/9506523 9506523]
</div>
<div class="pdbe-citations 1a66" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Doetsch, V.]]
[[Category: Doetsch V]]
[[Category: Sun, L J.]]
[[Category: Sun LJ]]
[[Category: Verdine, G L.]]
[[Category: Verdine GL]]
[[Category: Wagner, G.]]
[[Category: Wagner G]]
[[Category: Zhou, P.]]
[[Category: Zhou P]]
[[Category: Arre2]]
[[Category: Binary]]
[[Category: Binary complex]]
[[Category: Complex]]
[[Category: Enhanceosome]]
[[Category: Il-2]]
[[Category: Nfat]]
[[Category: Nfat/dna]]
[[Category: Nfat2]]
[[Category: Nfatc]]
[[Category: Nfatc1]]
[[Category: Nfatc1/dna]]
[[Category: Nmr]]
[[Category: Rel]]
[[Category: Transcription factor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:52:13 2008''

Latest revision as of 11:11, 22 May 2024

SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURESSOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES

Structural highlights

1a66 is a 3 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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

  1. Zhou P, Sun LJ, Dotsch V, Wagner G, Verdine GL. Solution structure of the core NFATC1/DNA complex. Cell. 1998 Mar 6;92(5):687-96. PMID:9506523
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