Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
- 1 June 1995
- journal article
- Published by Springer Nature in Nature
- Vol. 375 (6530) , 377-382
- https://doi.org/10.1038/375377a0
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.Keywords
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