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Journal Articles Nature Year : 1995

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

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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hal-03832776 , version 1 (27-10-2022)

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William Bourguet, Marc Ruff, Pierre Chambon, Hinrich Gronemeyer, Dino Moras. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature, 1995, 375 (6530), pp.377-382. ⟨10.1038/375377a0⟩. ⟨hal-03832776⟩
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