Nature. 1995 Jun 1;375(6530):377-82.

Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha.

Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D.

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Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP/Collège de France, Illkirch, CU de Strasbourg.

Abstract

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.

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Nature. 1995 Jun 1;375(6530):359-60.

PMID:: 7760929; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Ligand-Binding Domain Of The Human Nuclear Receptor Rxr- Alpha

PDB: 1LBD

Source: Homo sapiens

Method: X-Ray Diffraction

Resolution: 2.7 Å

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Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha.

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