2hb7: Difference between revisions

Revision as of 05:07, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2hb7.png

Template:STRUCTURE 2hb7

Crystal structure of VDR LBD in complex with 2alpha(3-hydroxy-1-propyl) calcitriolCrystal structure of VDR LBD in complex with 2alpha(3-hydroxy-1-propyl) calcitriol

Template:ABSTRACT PUBMED 16913708

About this StructureAbout this Structure

2HB7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Probing a water channel near the A-ring of receptor-bound 1 alpha,25-dihydroxyvitamin D3 with selected 2 alpha-substituted analogues., Hourai S, Fujishima T, Kittaka A, Suhara Y, Takayama H, Rochel N, Moras D, J Med Chem. 2006 Aug 24;49(17):5199-205. PMID:16913708

Page seeded by OCA on Tue Jul 29 05:07:39 2008

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OCA

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-'''Crystal structure of VDR LBD in complex with 2alpha(3-hydroxy-1-propyl) calcitriol'''
+===Crystal structure of VDR LBD in complex with 2alpha(3-hydroxy-1-propyl) calcitriol===
-==Overview==
+<!--
-The crystal structure of the vitamin D receptor (VDR) in complex with 1 alpha,25(OH)2D3 revealed the presence of several water molecules near the A-ring linking the ligand C-2 position to the protein surface. Here, we report the crystal structures of the human VDR ligand binding domain bound to selected C-2 alpha substituted analogues, namely, methyl, propyl, propoxy, hydroxypropyl, and hydroxypropoxy. These specific replacements do not modify the structure of the protein or the ligand, but with the exception of the methyl substituent, all analogues affect the presence and/or the location of the above water molecules. The integrity of the channel interactions and specific C-2 alpha analogue directed additional interactions correlate with the binding affinity of the ligands. In contrast, the resulting loss or gain of H-bonds does not reflect the magnitude of HL60 cell differentiation. Our overall findings highlight a rational approach to the design of more potent ligands by building in features revealed in the crystal structures.
+The line below this paragraph, {{ABSTRACT_PUBMED_16913708}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16913708 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16913708}}
 ==About this Structure==
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 [[Category: Rochel, N.]]
 [[Category: Alpha helical sandwich]]
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