2p7a

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[[Image:2p7a.jpg|left|200px]]
 
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==Crystal Structure of Estrogen Related Receptor g in complex with 3-methyl phenol==
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The line below this paragraph, containing "STRUCTURE_2p7a", creates the "Structure Box" on the page.
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<StructureSection load='2p7a' size='340' side='right'caption='[[2p7a]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2p7a]] is a 1 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=2P7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P7A FirstGlance]. <br>
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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]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=43M:4-CHLORO-3-METHYLPHENOL'>43M</scene></td></tr>
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{{STRUCTURE_2p7a| PDB=2p7a | SCENE= }}
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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=2p7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p7a OCA], [https://pdbe.org/2p7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p7a RCSB], [https://www.ebi.ac.uk/pdbsum/2p7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p7a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ERR3_HUMAN ERR3_HUMAN] Orphan receptor that acts as transcription activator in the absence of bound ligand. Binds specifically to an estrogen response element and activates reporter genes controlled by estrogen response elements (By similarity).<ref>PMID:19067653</ref> <ref>PMID:18063693</ref> <ref>PMID:11864604</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p7/2p7a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2p7a ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of Estrogen Related Receptor g in complex with 3-methyl phenol'''
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==See Also==
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*[[Estrogen-related receptor 3D structures|Estrogen-related receptor 3D structures]]
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== References ==
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==Overview==
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<references/>
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We screened the ligand-binding domain of estrogen-related receptor (ERR) gamma in ThermoFluor((R)), in an effort to develop chemical tools and decipher the biology of this orphan nuclear receptor. Several ligands were found to stabilize thermodynamically the protein. Amongst the ligands were bisphenol A (BPA) and 4-chloro-3-methyl phenol (ClCH(3)Ph). These ligands were further characterized and found to be competitive for 4-hydroxytamoxifen (4OHT) binding, a known reported antagonist ligand for ERRgamma, but functionally they did not enhance or disrupt affinity of the receptor for co-activator peptides. The preservation of the constitutive active conformation of the receptor in the presence of these two ligands was confirmed upon the determination of the co-crystal structures. The structures of BPA and ClCH(3)Ph were determined to a resolution of 2.1 and 2.3A, respectively, and the antagonist 4OHT was refined to 2.5A resolution. In the presence of BPA and ClCH(3)Ph the receptor maintained the transcriptional active conformation as reported previously for the apo-protein in the presence of a co-activator peptide fragment. In addition the ERRgamma-BPA structure identifies an interaction between the phenolic-OH and the side chain of N346. The preservation of the constitutive active conformation of the receptor in the presence of the small phenol compounds suggest that the biological activity of the receptor might be regulated by a natural occurring ligand.
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__TOC__
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</StructureSection>
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==About this Structure==
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2P7A 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=2P7A OCA].
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==Reference==
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Structural determination of estrogen-related receptor gamma in the presence of phenol derivative compounds., Abad MC, Askari H, O'Neill J, Klinger AL, Milligan C, Lewandowski F, Springer B, Spurlino J, Rentzeperis D, J Steroid Biochem Mol Biol. 2008 Jan;108(1-2):44-54. Epub 2007 Sep 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17964775 17964775]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Abad, M C.]]
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[[Category: Abad MC]]
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[[Category: Hormone receptor]]
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[[Category: Three layered alpha helical sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:32:29 2008''
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Current revision

Crystal Structure of Estrogen Related Receptor g in complex with 3-methyl phenol

PDB ID 2p7a

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