4q0a: Difference between revisions
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<StructureSection load='4q0a' size='340' side='right'caption='[[4q0a]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4q0a' size='340' side='right'caption='[[4q0a]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4q0a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4q0a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q0A FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4OA:(3BETA,5BETA,14BETA,17ALPHA)-3-HYDROXYCHOLAN-24-OIC+ACID'>4OA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4OA:(3BETA,5BETA,14BETA,17ALPHA)-3-HYDROXYCHOLAN-24-OIC+ACID'>4OA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4q0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0a OCA], [https://pdbe.org/4q0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q0a RCSB], [https://www.ebi.ac.uk/pdbsum/4q0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q0a ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4q0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0a OCA], [https://pdbe.org/4q0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q0a RCSB], [https://www.ebi.ac.uk/pdbsum/4q0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q0a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/VDRA_DANRE VDRA_DANRE] Nuclear hormone receptor. Transcription factor that mediates the action of vitamin D3 by controlling the expression of hormone sensitive genes. Regulates transcription of hormone sensitive genes via its association with the WINAC complex, a chromatin-remodeling complex. Plays a central role in calcium homeostasis.<ref>PMID:17218092</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Danio rerio]] | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Belorusova | [[Category: Belorusova A]] | ||
[[Category: Rochel | [[Category: Rochel N]] | ||
Revision as of 10:39, 8 February 2023
Vitamin D Receptor complex with lithocholic acidVitamin D Receptor complex with lithocholic acid
Structural highlights
FunctionVDRA_DANRE Nuclear hormone receptor. Transcription factor that mediates the action of vitamin D3 by controlling the expression of hormone sensitive genes. Regulates transcription of hormone sensitive genes via its association with the WINAC complex, a chromatin-remodeling complex. Plays a central role in calcium homeostasis.[1] Publication Abstract from PubMedThe vitamin D receptor (VDR), an endocrine nuclear receptor for 1alpha,25-dihydroxyvitamin D3, acts also as a bile acid sensor by binding lithocholic acid (LCA). The crystal structure of the zebrafish VDR ligand binding domain in complex with LCA and the SRC-2 coactivator peptide reveals the binding of two LCA molecules by VDR. One LCA binds to the canonical ligand-binding pocket, and the second one, which is not fully buried, is anchored to a site located on the VDR surface. Despite the low affinity of the alternative site, the binding of the second molecule promotes stabilization of the active receptor conformation. Biological activity assays, structural analysis, and molecular dynamics simulations indicate that the recognition of two ligand molecules is crucial for VDR agonism by LCA. The unique binding mode of LCA provides clues for the development of new chemical compounds that target alternative binding sites for therapeutic applications. Structural insights into the molecular mechanism of vitamin d receptor activation by lithocholic Acid involving a new mode of ligand recognition.,Belorusova AY, Eberhardt J, Potier N, Stote RH, Dejaegere A, Rochel N J Med Chem. 2014 Jun 12;57(11):4710-9. doi: 10.1021/jm5002524. Epub 2014 May 21. PMID:24818857[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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