6lit

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Current revision (11:00, 22 November 2023) (edit) (undo)
 
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==Estrogen-related receptor beta(ERR2) in complex with BPA==
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<StructureSection load='6lit' size='340' side='right'caption='[[6lit]]' scene=''>
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<StructureSection load='6lit' size='340' side='right'caption='[[6lit]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6lit]] is a 4 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=6LIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LIT FirstGlance]. <br>
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</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=6lit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lit OCA], [http://pdbe.org/6lit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lit RCSB], [http://www.ebi.ac.uk/pdbsum/6lit PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lit ProSAT]</span></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]] 2&#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=2OH:4,4-PROPANE-2,2-DIYLDIPHENOL'>2OH</scene></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=6lit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lit OCA], [https://pdbe.org/6lit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lit RCSB], [https://www.ebi.ac.uk/pdbsum/6lit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lit ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ERR2_HUMAN ERR2_HUMAN] Defects in ESRRB are the cause of deafness autosomal recessive type 35 (DFNB35) [MIM:[https://omim.org/entry/608565 608565]. DFNB35 is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.<ref>PMID:18179891</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/ERR2_HUMAN ERR2_HUMAN] Nuclear receptor, may regulate ESR1 transcriptional activity.<ref>PMID:19755138</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Estrogen-related receptor beta (ERRbeta) is a nuclear receptor critical for many biological processes. Despite the biological and pharmaceutical importance of ERRbeta, deciphering the structure of ERRbeta has been hampered by the difficulties in obtaining a pure and stable protein for structural studies. In fact, the ERRbeta ligand-binding domain remains the last unsolved ERR structure and also one of only a few unknown nuclear receptor structures. Here, we report the identification of a critical single-residue mutation resulted in robust solubility and stability of an active ERRbeta ligand-binding domain, thereby providing a protein tool enabling the first probe into the biochemical and structural studies of this important receptor. The crystal structure reveals key structural features that have enabled the integration of the molecular determinants of signals transduced across the ligand binding and coregulator recruitment by all three ERR subtypes, which also provides a framework for the rational design of selective and potent ligands for the treatment of various ERR-mediated diseases.
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Structural Insights into the Specificity of Ligand Binding and Coactivator Assembly by Estrogen-Related Receptor beta.,Yao B, Zhang S, Wei Y, Tian S, Lu Z, Jin L, He Y, Xie W, Li Y J Mol Biol. 2020 Sep 4;432(19):5460-5472. doi: 10.1016/j.jmb.2020.08.007. Epub, 2020 Aug 12. PMID:32795533<ref>PMID:32795533</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 6lit" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Z-disk]]
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[[Category: Li Y]]
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[[Category: Yao BQ]]

Current revision

Estrogen-related receptor beta(ERR2) in complex with BPA

PDB ID 6lit

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