Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
