3o1d
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3o1d]] 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=3O1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O1D FirstGlance]. <br> | <table><tr><td colspan='2'>[[3o1d]] 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=3O1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O1D FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G72:(1R,3R,7E,17BETA)-17-[(1S)-6,6,6-TRIFLUORO-5-HYDROXY-1-(4-HYDROXY-4-METHYLPENTYL)-5-(TRIFLUOROMETHYL)HEX-3-YN-1-YL]-9,10-SECOESTRA-5,7-DIENE-1,3-DIOL'>G72</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4007Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G72:(1R,3R,7E,17BETA)-17-[(1S)-6,6,6-TRIFLUORO-5-HYDROXY-1-(4-HYDROXY-4-METHYLPENTYL)-5-(TRIFLUOROMETHYL)HEX-3-YN-1-YL]-9,10-SECOESTRA-5,7-DIENE-1,3-DIOL'>G72</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=3o1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o1d OCA], [https://pdbe.org/3o1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o1d RCSB], [https://www.ebi.ac.uk/pdbsum/3o1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o1d 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=3o1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o1d OCA], [https://pdbe.org/3o1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o1d RCSB], [https://www.ebi.ac.uk/pdbsum/3o1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o1d 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> | [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;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Derivatives of vitamin D(3) containing a second side-chain emanating at C-20 are known as gemini and act as vitamin D receptor agonists. Recently, two of these, namely Gemini-0072 and the epimeric Gemini-0097, were selected for further studies in view of their high biological activities and lack of hypercalcemic effects. We now show that the two analogs recruit coactivator SRC-1 better than the parental gemini and act as VDR superagonists. The crystal structures of complexes of zVDR with Gemini-0072 and Gemini-0097 indicate that these ligands induce an extra cavity within the ligand-binding pocket similar to gemini and that their superagonistic activity is due to an increased stabilization of helix H12. | ||
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| - | Structure-function study of gemini derivatives with two different side chains at C-20, Gemini-0072 and Gemini-0097.,Huet T, Maehr H, Lee HJ, Uskokovic MR, Suh N, Moras D, Rochel N Medchemcomm. 2011;2(5):424-429. PMID:22180837<ref>PMID:22180837</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3o1d" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structure-function study of Gemini derivatives with two different side chains at C-20, Gemini-0072 and Gemini-0097.
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