The translocator protein (TSPO), an 18-kDa transmembrane protein primarily found in the outer mitochondrial membrane, is evolutionarily conserved and widely distributed across species. In mammals, TSPO has been described as a key member of a multiprotein complex involved in many putative functions and, over the years, several classes of ligand have been developed to modulate these functions. In this review, we consider the currently available atomic structures of mouse and bacterial TSPO and propose a rationale for the development of new ligands for the protein. We provide a review of TSPO monomeric and oligomeric states and their conformational flexibility, together with ligand-binding site and interaction mechanisms. These data are expected to help considerably the development of high-affinity ligands for TSPO-based therapies or diagnostics.

中文翻译：

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深入了解 TSPO 的结构特征：对药物开发的影响。


易位蛋白 (TSPO) 是一种 18 kDa 跨膜蛋白，主要存在于线粒体外膜中，在进化上是保守的，并且广泛分布于各个物种。在哺乳动物中，TSPO 被描述为涉及许多假定功能的多蛋白复合物的关键成员，多年来，已经开发了几类配体来调节这些功能。在这篇综述中，我们考虑了小鼠和细菌 TSPO 目前可用的原子结构，并提出了开发该蛋白质新配体的基本原理。我们综述了 TSPO 单体和寡聚状态及其构象灵活性，以及​​配体结合位点和相互作用机制。这些数据预计将大大有助于基于 TSPO 的治疗或诊断的高亲和力配体的开发。