G蛋白偶联受体寡聚体结构研究进展  

Structure of G Protein-Coupled Receptor Oligomers

作　　者：薛礼[1] 赵菡[1] 刘俊科[1] 邹伦浩 刘林青[2] 黄思罗[1] 

机构地区：[1]华中科技大学生命科学与技术学院,分子生物物理教育部重点实验室,湖北武汉430074 [2]武汉大学中国产学研究合作问题研究中心,湖北武汉430072

出　　处：《现代生物医学进展》2015年第8期1547-1552,共6页Progress in Modern Biomedicine

基　　金：第47批中国博士后面上基金(20100471184);国家自然科学基金面上项目(30973514)

摘　　要：G蛋白偶联受体(GPCR)是细胞膜上最大的一类受体,其通过构象变化激活下游G蛋白从而介导细胞响应多种来自内源和外界环境中的信号。自GPCR被发现以来,研究者就一直在努力解析GPCR的构象,x射线晶体衍射技术和GPCR蛋白质结晶技术的发展使得越来越多的GPCR单体在静息状态,以及与不同配体甚至G蛋白结合的晶体结构被成功解析。另一方面,FRET和电子显微技术的运用得到了GPCR二聚化和多聚化的多方面证据。本文将结合近年来该领域的进展,对GPCR寡聚体的结构和构象变化予以系统的综述,这些成果为研究GPCR的功能机制及其特异性的靶点药物开发提供了重要的基础。G protein-coupled receptors（GPCR） are the largest class of cell membrane receptors. As a sensor of cells, GPCR mediated a variety of signals from endogenous and external environment. GPCR activated downstream G proteins for signal transduction through conformational changes. Since GPCR was found, researchers have been trying to resolve GPCR structure conformation,multifaceted evidence of GPCR dimerization and oligomerization was obtained using tr FRET and electron microscopy technique. And x-ray crystal diffraction and GPCR protein crystallization technology made more GPCR crystal structure was successfully resolved to obtain the high-precision three-dimensional structure. As the developing of technology, GPCR crystal structure with different ligands or G protein binding further demonstrates different state of GPCR conformations. These results had laid an important foundation for the study of GPCR function mechanisms and drug development with specific targets. This article reviewed GPCR structures in recent years.

关 键 词：G蛋白偶联受体 二聚化 寡聚化 晶体结构 

分 类 号：Q25[生物学—细胞生物学] Q27