Renaud J P, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D
Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP/Collège de France, Strasbourg, France.
Nature. 1995 Dec 14;378(6558):681-9. doi: 10.1038/378681a0.
The 2.0-A crystal structure of the ligand-binding domain (LBD) of the human retinoic acid receptor (RAR)-gamma bound to all-trans retinoic acid reveals the ligand-binding interactions and suggests an electrostatic guidance mechanism. The overall fold is similar to that of the human RXR-alpha apo-LBD, except for the carboxy-terminal part which folds back towards the LBD core, contributing to the hydrophobic ligand pocket and 'sealing' its entry site. We propose a 'mouse trap' mechanism whereby a ligand-induced conformational transition repositions the amphipathic alpha-helix of the AF-2 activating domain and forms a transcriptionally active receptor.
人视黄酸受体（RAR）-γ 配体结合结构域（LBD）与全反式视黄酸结合的 2.0 埃晶体结构揭示了配体结合相互作用，并提示了一种静电引导机制。除了羧基末端部分向 LBD 核心折回，形成疏水配体口袋并 “封闭” 其入口位点外，整体折叠结构与人 RXR-α 无配体 LBD 相似。我们提出了一种 “捕鼠器” 机制，即配体诱导的构象转变重新定位 AF-2 激活结构域的两亲性 α 螺旋，形成转录活性受体。
