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, 375 (6530), 377-82

Crystal Structure of the Ligand-Binding Domain of the Human Nuclear Receptor RXR-alpha

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Crystal Structure of the Ligand-Binding Domain of the Human Nuclear Receptor RXR-alpha

W Bourguet et al. Nature.

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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