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1lbd

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1lbd, resolution 2.7Å

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LIGAND-BINDING DOMAIN OF THE HUMAN NUCLEAR RECEPTOR RXR-ALPHA

Overview

The crystal structure of the human retinoid-X receptor RXR-alpha ligand-binding domain reveals a previously undiscovered fold of an antiparallel alpha-helical sandwich, packed as dimeric units. Two helices and one loop form the homodimerization surface, and hydrophobic heptad repeats participate in stabilizing the fold. The existence of a ligand-binding pocket is proposed that would allow 9-cis retinoic acid to interact with different functional modules, including the AF-2 activating domain. Several lines of evidence indicate that the overall structure is a prototype fold of ligand-binding domains of nuclear receptors.

About this Structure

1LBD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha., Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D, Nature. 1995 Jun 1;375(6530):377-82. PMID:7760929

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