1pzu

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Current revision (09:00, 21 February 2024) (edit) (undo)
 
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<StructureSection load='1pzu' size='340' side='right'caption='[[1pzu]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='1pzu' size='340' side='right'caption='[[1pzu]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1pzu]] is a 12 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=1PZU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PZU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1pzu]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PZU FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a02|1a02]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NFAT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1pzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pzu OCA], [https://pdbe.org/1pzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pzu RCSB], [https://www.ebi.ac.uk/pdbsum/1pzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pzu ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1pzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pzu OCA], [http://pdbe.org/1pzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pzu RCSB], [http://www.ebi.ac.uk/pdbsum/1pzu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pzu ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[https://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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1pzu ConSurf].
</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=1pzu ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The crystal structure of the NFAT1 Rel homology region (RHR) bound to a pseudo-palindromic DNA site reveals an asymmetric dimer interaction between the RHR-C domains, unrelated to the contact seen in Rel dimers such as NF kappa B. Binding studies with a form of the NFAT1 RHR defective in the dimer contact show loss of cooperativity and demonstrate that the same interaction is present in solution. The structure we have determined may correspond to a functional NFAT binding mode at palindromic sites of genes induced during the anergic response to weak TCR signaling.
 
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An asymmetric NFAT1 dimer on a pseudo-palindromic kappa B-like DNA site.,Jin L, Sliz P, Chen L, Macian F, Rao A, Hogan PG, Harrison SC Nat Struct Biol. 2003 Oct;10(10):807-11. Epub 2003 Aug 31. PMID:12949491<ref>PMID:12949491</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1pzu" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, L]]
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[[Category: Chen L]]
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[[Category: Harrison, S C]]
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[[Category: Harrison SC]]
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[[Category: Hogan, P G]]
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[[Category: Hogan PG]]
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[[Category: Jin, L]]
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[[Category: Jin L]]
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[[Category: Macian, F]]
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[[Category: Macian F]]
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[[Category: Rao, A]]
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[[Category: Rao A]]
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[[Category: Sliz, P]]
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[[Category: Sliz P]]
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[[Category: Human il8 promoter]]
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[[Category: Nfat1-rhr homodimer]]
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[[Category: Protein-dna complex]]
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[[Category: Transcription factor]]
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[[Category: Transcription-dna complex]]
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Current revision

An asymmetric NFAT1-RHR homodimer on a pseudo-palindromic, Kappa-B site

PDB ID 1pzu

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