2awh: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2awh]] is a 2 chain structure with 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=2AWH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AWH FirstGlance]. <br> | <table><tr><td colspan='2'>[[2awh]] is a 2 chain structure with 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=2AWH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AWH FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B7G:HEPTYL-BETA-D-GLUCOPYRANOSIDE'>B7G</scene>, <scene name='pdbligand=VCA:VACCENIC+ACID'>VCA</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B7G:HEPTYL-BETA-D-GLUCOPYRANOSIDE'>B7G</scene>, <scene name='pdbligand=VCA:VACCENIC+ACID'>VCA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2awh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2awh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2awh RCSB], [http://www.ebi.ac.uk/pdbsum/2awh PDBsum]</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=2awh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2awh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2awh RCSB], [http://www.ebi.ac.uk/pdbsum/2awh PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Alphey, M S | [[Category: Alphey, M S]] | ||
[[Category: Bjorkling, F | [[Category: Bjorkling, F]] | ||
[[Category: Buetow, L | [[Category: Buetow, L]] | ||
[[Category: Ferguson, M A.J | [[Category: Ferguson, M A.J]] | ||
[[Category: Fyffe, S A | [[Category: Fyffe, S A]] | ||
[[Category: Hunter, W N | [[Category: Hunter, W N]] | ||
[[Category: Smith, T K | [[Category: Smith, T K]] | ||
[[Category: Sorensen, M D | [[Category: Sorensen, M D]] | ||
[[Category: Gene regulation]] | [[Category: Gene regulation]] | ||
[[Category: Nuclear receptor]] | [[Category: Nuclear receptor]] | ||
[[Category: Ppar]] | [[Category: Ppar]] | ||
[[Category: Protein-ligand complex]] | [[Category: Protein-ligand complex]] | ||
Revision as of 12:54, 8 January 2015
Human Nuclear Receptor-Ligand Complex 1Human Nuclear Receptor-Ligand Complex 1
Structural highlights
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 PubMedHigh-resolution crystallographic structures of recombinant human peroxisome proliferator-activated receptor ligand-binding domain (isotype beta/delta) reveal a fatty acid in the binding site. Mass spectrometry confirmed the presence of C16:0, C16:1, C18:0 and C18:1 in a ratio of approximately 3:2:1:4 with 11, Z-octadecenoic acid (cis-vaccenic acid) identified as the predominant species. These are endogenous fatty acids acquired from the bacterial expression system, and serve to lock the ligand-binding domain into the activated conformation. A requirement for crystal growth, the additive n-heptyl-beta-d-glucopyranoside, binds near the activation function helix where recognition of co-activator proteins occurs. Our observations suggest potential physiological ligands for human PPAR-beta/delta and highlight that reported binding studies must be treated with caution unless endogenous fatty acids have been removed from the sample prior to analysis. Recombinant human PPAR-beta/delta ligand-binding domain is locked in an activated conformation by endogenous fatty acids.,Fyffe SA, Alphey MS, Buetow L, Smith TK, Ferguson MA, Sorensen MD, Bjorkling F, Hunter WN J Mol Biol. 2006 Mar 3;356(4):1005-13. Epub 2006 Jan 4. PMID:16405912[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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