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spinqualitylabelsall models PDB ID 1fd0 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.38Å
Ligands:	and
Coordinates:	save as pdb, mmCIF, xml

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. 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

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