3aun: Difference between revisions
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[[ | ==Crystal structure of the rat vitamin D receptor ligand binding domain complexed with YR335 and a synthetic peptide containing the NR2 box of DRIP 205== | ||
<StructureSection load='3aun' size='340' side='right' caption='[[3aun]], [[Resolution|resolution]] 1.81Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3aun]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AUN FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=YR4:(2R)-2-{4-[3-(4-{[(2R)-2-HYDROXY-3,3-DIMETHYLBUTYL]OXY}-3-METHYLPHENYL)PENTAN-3-YL]-2-METHYLPHENOXY}BUTANE-1,4-DIOL'>YR4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zfx|2zfx]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aun RCSB], [http://www.ebi.ac.uk/pdbsum/3aun PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We designed and synthesized nonsecosteroidal vitamin D receptor (VDR) ligands that formed H-bonds with six amino acid residues (Tyr143, Ser233, Arg270, Ser274, His301 and His393) of the VDR ligand-binding domain. The ligand YR335 exhibited potent transcriptional activity, which was comparable to those of 1alpha,25-dihydroxyvitamin D(3) and YR301. The crystal structure of the complex formed between YR335 and the VDR ligand-binding domain was solved, which revealed that YR335 formed H-bonds with the six amino acid residues mentioned above. | |||
Design, synthesis and X-ray crystallographic study of new nonsecosteroidal vitamin D receptor ligands.,Demizu Y, Takahashi T, Kaneko F, Sato Y, Okuda H, Ochiai E, Horie K, Takagi K, Kakuda S, Takimoto-Kamimura M, Kurihara M Bioorg Med Chem Lett. 2011 Oct 15;21(20):6104-7. Epub 2011 Aug 17. PMID:21889334<ref>PMID:21889334</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Sandbox vdr|Sandbox vdr]] | |||
*[[Vitamin D receptor|Vitamin D receptor]] | *[[Vitamin D receptor|Vitamin D receptor]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Kakuda, S.]] | [[Category: Kakuda, S.]] | ||
Revision as of 09:18, 5 November 2014
Crystal structure of the rat vitamin D receptor ligand binding domain complexed with YR335 and a synthetic peptide containing the NR2 box of DRIP 205
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