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

机译:人核受体RXR-alpha的配体结合结构域的晶体结构。

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摘要

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.
机译:人类视黄醇X受体RXR-α配体结合域的晶体结构揭示了反平行的α-螺旋夹心的先前未发现的折叠,以二聚体单位包装。两个螺旋和一个环形成均二聚化表面,并且疏水七肽重复序列参与稳定折叠。提出了配体结合袋的存在,其将允许9-顺式视黄酸与包括AF-2活化域的不同功能模块相互作用。几条证据表明,总体结构是核受体配体结合域的原型折叠。

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