1p7h

<table><tr><td colspan='2'>[[1p7h]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P7H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P7H FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NFATC2 OR NFAT1 OR NFATP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1p7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p7h OCA], [http://pdbe.org/1p7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p7h RCSB], [http://www.ebi.ac.uk/pdbsum/1p7h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p7h ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/NFAC2_HUMAN NFAC2_HUMAN]] Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway.<ref>PMID:21871017</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

DNA binding by NFAT1 as a dimer has been implicated in the activation of host and viral genes. Here we report a crystal structure of NFAT1 bound cooperatively as a dimer to the highly conserved kappa B site from the human immunodeficiency virus 1 (HIV-1) long terminal repeat (LTR). This structure reveals a new mode of dimerization and protein-DNA recognition by the Rel homology region (RHR) of NFAT1. The two NFAT1 monomers form a complete circle around the kappa B DNA through protein-protein interactions mediated by both their N- and C-terminal subdomains. The major dimer interface, formed by the C-terminal domain, is asymmetric and substantially different from the symmetric dimer interface seen in other Rel family proteins. Comparison to other NFAT structures, including NFAT5 and the NFAT1-Fos-Jun-ARRE2 complex, reveals that NFAT1 adopts different conformations and its protein surfaces mediate distinct protein-protein interactions in the context of different DNA sites.

Structure of NFAT1 bound as a dimer to the HIV-1 LTR kappa B element.,Giffin MJ, Stroud JC, Bates DL, von Koenig KD, Hardin J, Chen L Nat Struct Biol. 2003 Oct;10(10):800-6. Epub 2003 Aug 31. PMID:12949493<ref>PMID:12949493</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1p7h" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Bates, D L]]

[[Category: Chen, L]]

[[Category: Giffin, M J]]

[[Category: Hardin, J]]

[[Category: Koenig, K D.von]]

[[Category: Stroud, J C]]

[[Category: Activator]]

[[Category: Transcription-dna complex]]