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1fd0

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(New page: 200px<br /> <applet load="1fd0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fd0, resolution 1.38&Aring;" /> '''ISOTYPE SELECTIVITY...)
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Revision as of 14:45, 12 November 2007

Image:1fd0.gif

1fd0, resolution 1.38Å

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ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254

Overview

Hydrogen bonds between polarized atoms play a crucial role in protein, interactions and are often used in drug design, which usually neglects the, potential of C-H...O hydrogen bonds. The 1.4 A resolution crystal, structure of the ligand binding domain of the retinoic acid receptor, RARgamma complexed with the retinoid SR11254 reveals several types of, C-H...O hydrogen bonds. A striking example is the hydroxyl group of the, ligand that acts as an H bond donor and acceptor, leading to a synergy, between classical and C-H...O hydrogen bonds. This interaction introduces, both specificity and affinity within the hydrophobic ligand pocket. The, similarity of intraprotein and protein-ligand C-H...O interactions, suggests that such bonds should be considered in rational drug design, approaches.

About this Structure

1FD0 is a Single protein structure of sequence from Homo sapiens with 254 and LMU as ligands. Full crystallographic information is available from OCA.

Reference

C-H...O hydrogen bonds in the nuclear receptor RARgamma--a potential tool for drug selectivity., Klaholz B, Moras D, Structure. 2002 Sep;10(9):1197-204. PMID:12220491

Page seeded by OCA on Mon Nov 12 16:51:45 2007

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