3ax8

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[[Image:3ax8.jpg|left|200px]]
 
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==Crystal structure of the human vitamin D receptor ligand binding domain complexed with 15alpha-methoxy-1alpha,25-dihydroxyvitamin D3==
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The line below this paragraph, containing "STRUCTURE_3ax8", creates the "Structure Box" on the page.
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<StructureSection load='3ax8' size='340' side='right'caption='[[3ax8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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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'>[[3ax8]] 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=3AX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AX8 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]] 2.6&#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=EIM:(1R,3S,5Z)-5-[(2E)-2-[(1R,3S,3AS,7AR)-1-[(2R)-6-HYDROXY-6-METHYL-HEPTAN-2-YL]-3-METHOXY-7A-METHYL-2,3,3A,5,6,7-HEXAHYDRO-1H-INDEN-4-YLIDENE]ETHYLIDENE]-4-METHYLIDENE-CYCLOHEXANE-1,3-DIOL'>EIM</scene></td></tr>
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{{STRUCTURE_3ax8| PDB=3ax8 | 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=3ax8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ax8 OCA], [https://pdbe.org/3ax8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ax8 RCSB], [https://www.ebi.ac.uk/pdbsum/3ax8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ax8 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/VDR_HUMAN VDR_HUMAN] Defects in VDR are the cause of rickets vitamin D-dependent type 2A (VDDR2A) [MIM:[https://omim.org/entry/277440 277440]. A disorder of vitamin D metabolism resulting in severe rickets, hypocalcemia and secondary hyperparathyroidism. Most patients have total alopecia in addition to rickets.<ref>PMID:2849209</ref> <ref>PMID:8381803</ref> <ref>PMID:1652893</ref> <ref>PMID:2177843</ref> <ref>PMID:8106618</ref> <ref>PMID:8392085</ref> <ref>PMID:7828346</ref> <ref>PMID:8675579</ref> <ref>PMID:8961271</ref> <ref>PMID:9005998</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/VDR_HUMAN VDR_HUMAN] 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. Recruited to promoters via its interaction with the WINAC complex subunit BAZ1B/WSTF, which mediates the interaction with acetylated histones, an essential step for VDR-promoter association. Plays a central role in calcium homeostasis.<ref>PMID:16252006</ref> <ref>PMID:10678179</ref> <ref>PMID:15728261</ref> <ref>PMID:16913708</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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C15-Substituted 1alpha,25-dihydroxyvitamin D(3) analogs were synthesized for the first time to investigate the effects of the modified CD-ring on biological activity concerning the agonistic positioning of helix-3 and helix-12 of the vitamin D receptor (VDR). X-ray cocrystallographic analysis proved that 0.6 A shifts of the CD-ring and shrinking of the side chain were necessary to maintain the position of the 25-hydroxy group for proper interaction with helix-12. The 15-hydroxy-16-ene derivative showed higher binding affinity for hVDR than the natural hormone.
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===Crystal structure of the human vitamin D receptor ligand binding domain complexed with 15alpha-methoxy-1alpha,25-dihydroxyvitamin D3===
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New C15-substituted active vitamin D3.,Shindo K, Kumagai G, Takano M, Sawada D, Saito N, Saito H, Kakuda S, Takagi K, Ochiai E, Horie K, Takimoto-Kamimura M, Ishizuka S, Takenouchi K, Kittaka A Org Lett. 2011 Jun 3;13(11):2852-5. Epub 2011 May 3. PMID:21539305<ref>PMID:21539305</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 3ax8" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_21539305}}, adds the Publication Abstract to the page
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*[[Sandbox vdr|Sandbox vdr]]
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(as it appears on PubMed at http://www.pubmed.gov), where 21539305 is the PubMed ID number.
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*[[Vitamin D receptor 3D structures|Vitamin D receptor 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_21539305}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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[[3ax8]] is a 1 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=3AX8 OCA].
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==Reference==
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<ref group="xtra">PMID:021539305</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Kakuda, S.]]
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[[Category: Large Structures]]
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[[Category: Takimoto-Kamimura, M.]]
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[[Category: Kakuda S]]
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[[Category: Hormone receptor]]
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[[Category: Takimoto-Kamimura M]]
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[[Category: Transcription]]
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Current revision

Crystal structure of the human vitamin D receptor ligand binding domain complexed with 15alpha-methoxy-1alpha,25-dihydroxyvitamin D3

PDB ID 3ax8

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