摘要
背景：大麻素受体1（CB1）是一种在中枢神经系统中普遍存在的膜蛋白，其结晶结构最近已得到解决。需要研究CB1配合物及其配体及其在新药开发中的作用。目标：我们的目标是回顾CB1的研究，从一般方面开始，重点关注最近的结构研究，重点是反向激动剂结合结构。 方法：我们从文献综述开始，然后我们描述最近关于CB 1晶体结构和对接模拟的研究。我们使用这种结构信息来描述蛋白质 - 配体相互作用。我们还描述了用反向激动剂获得CB 1的复杂结构的分子对接方法。 结果：结晶结构和对接结果的分析揭示了负反义激动剂对CB1的特异性的残基。大多数分子间相互作用涉及疏水残基，所有复杂结构中残基Phe 170和Leu 359的参与在目前的研究中。对于具有otenabant和taranabant的复合物，我们观察到涉及残基His 178（otenabant）和Thr 197和Ser 383（taranabant）的分子间氢键。 结论：对反向激动剂和CB 1结构的分析揭示了残基Phe 170和Leu 359在它们的相互作用中发挥的关键作用和强的分子间氢键，突出了在新型反向激动剂的开发中探索分子间相互作用的重要性。
关键词: 大麻素受体，药物设计，对接，反向激动剂，膜蛋白，GPCR。
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