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X-ray Crystal Structure of the Liver X Receptor β Ligand Binding Domain
Journal of Biological Chemistry
The x-ray crystal structures of the human liver X receptor ␤ ligand binding domain complexed to sterol and nonsterol agonists revealed a perpendicular histidinetryptophan switch that holds the receptor in its active conformation. Hydrogen bonding interactions with the ligand act to position the His-435 imidazole ring against the Trp-457 indole ring, allowing an electrostatic interaction that holds the AF2 helix in the active position. The neutral oxysterol 24(S),25-epoxycholesterol accepts adoi:10.1074/jbc.m302260200 pmid:12736258 fatcat:4fva3fhqhjctdbgyxgjaecsgmu