7qpp - Revision history

OCA at 13:20, 1 February 2024

OCA — Thu, 01 Feb 2024 13:20:54 GMT

←Older revision		Revision as of 13:20, 1 February 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7qpp]] 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=7QPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPP FirstGlance]. <br>		<table><tr><td colspan='2'>[[7qpp]] 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=7QPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=VDX:5-{2-[1-(5-HYDROXY-1,5-DIMETHYL-HEXYL)-7A-METHYL-OCTAHYDRO-INDEN-4-YLIDENE]-ETHYLIDENE}-4-METHYLENE-CYCLOHEXANE-1,3-DIOL'>VDX</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]] 1.52Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=VDX:5-{2-[1-(5-HYDROXY-1,5-DIMETHYL-HEXYL)-7A-METHYL-OCTAHYDRO-INDEN-4-YLIDENE]-ETHYLIDENE}-4-METHYLENE-CYCLOHEXANE-1,3-DIOL'>VDX</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=7qpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpp OCA], [https://pdbe.org/7qpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpp RCSB], [https://www.ebi.ac.uk/pdbsum/7qpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpp 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=7qpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpp OCA], [https://pdbe.org/7qpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpp RCSB], [https://www.ebi.ac.uk/pdbsum/7qpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpp ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:50, 28 December 2022

OCA — Wed, 28 Dec 2022 08:50:14 GMT

←Older revision		Revision as of 08:50, 28 December 2022
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7qpp is ~~ON HOLD until Paper~~ Publication	+	==High resolution structure of human VDR ligand binding domain in complex with calcitriol==
		+	<StructureSection load='7qpp' size='340' side='right'caption='[[7qpp]], [[Resolution\|resolution]] 1.52Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[7qpp]] 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=7QPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPP FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=VDX:5-{2-[1-(5-HYDROXY-1,5-DIMETHYL-HEXYL)-7A-METHYL-OCTAHYDRO-INDEN-4-YLIDENE]-ETHYLIDENE}-4-METHYLENE-CYCLOHEXANE-1,3-DIOL'>VDX</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=7qpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpp OCA], [https://pdbe.org/7qpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpp RCSB], [https://www.ebi.ac.uk/pdbsum/7qpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpp ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[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>
		+	== Function ==
		+	[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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	1alpha,25-dihydroxyvitamin D3 (1,25D(3)) regulates many physiological processes in vertebrates by binding to the vitamin D receptor (VDR). Phylogenetic analysis indicates that jawless fishes are the most basal vertebrates exhibiting a VDR gene. To elucidate the mechanism driving VDR activation during evolution, we determined the crystal structure of the VDR ligand-binding domain (LBD) complex from the basal vertebratePetromyzon marinus, sea lamprey (lVDR). Comparison of three-dimensional crystal structures of the lVDR-1,25D(3) complex with higher vertebrate VDR-1,25D(3) structures suggests that 1,25D(3) binds to lVDR similarly to human VDR, but with unique features for lVDR around linker regions between H11 and H12 and between H9 and H10. These structural differences may contribute to the marked species differences in transcriptional responses. Furthermore, residue co-evolution analysis of VDR across vertebrates identifies amino acid positions in H9 and the large insertion domain VDR LBD specific as correlated.

-	~~Authors~~:	+	Advances in Vitamin D Receptor Function and Evolution Based on the 3D Structure of the Lamprey Ligand-Binding Domain.,Sigueiro R, Bianchetti L, Peluso-Iltis C, Chalhoub S, Dejaegere A, Osz J, Rochel N J Med Chem. 2022 Apr 14;65(7):5821-5829. doi: 10.1021/acs.jmedchem.2c00171. Epub , 2022 Mar 18. PMID:35302785<ref>PMID:35302785</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 7qpp" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
		+	[[Category: Rochel N]]

OCA: Protected "7qpp" [edit=sysop:move=sysop]

OCA — Wed, 12 Jan 2022 08:31:44 GMT

Protected "7qpp" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:31, 12 January 2022

OCA: New page: '''Unreleased structure''' The entry 7qpp is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

OCA — Wed, 12 Jan 2022 08:31:43 GMT

New page: '''Unreleased structure''' The entry 7qpp is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7qpp is ON HOLD until Paper Publication

Authors:

Description:
[[Category: Unreleased Structures]]