Moreira Irina S
REQUIMTE/Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade do Porto, Rua do Campo Alegre s/n, 4169-007 Porto, Portugal.
Biochim Biophys Acta. 2014 Jan;1840(1):16-33. doi: 10.1016/j.bbagen.2013.08.027. Epub 2013 Sep 7.
The details of the functional interaction between G proteins and the G protein coupled receptors (GPCRs) have long been subjected to extensive investigations with structural and functional assays and a large number of computational studies.
The nature and sites of interaction in the G-protein/GPCR complexes, and the specificities of these interactions selecting coupling partners among the large number of families of GPCRs and G protein forms, are still poorly defined.
Many of the contact sites between the two proteins in specific complexes have been identified, but the three dimensional molecular architecture of a receptor-Gα interface is only known for one pair. Consequently, many fundamental questions regarding this macromolecular assembly and its mechanism remain unanswered.
In the context of current structural data we review the structural details of the interfaces and recognition sites in complexes of sub-family A GPCRs with cognate G-proteins, with special emphasis on the consequences of activation on GPCR structure, the prevalence of preassembled GPCR/G-protein complexes, the key structural determinants for selective coupling and the possible involvement of GPCR oligomerization in this process.
长期以来，人们一直通过结构和功能分析以及大量的计算研究，对G蛋白与G蛋白偶联受体（GPCRs）之间的功能相互作用细节进行广泛研究。
G蛋白/GPCR复合物中相互作用的性质和位点，以及这些相互作用在众多GPCR家族和G蛋白形式中选择偶联伙伴的特异性，仍然定义不明确。
已确定了特定复合物中两种蛋白质之间的许多接触位点，但仅一对受体-Gα界面的三维分子结构是已知的。因此，关于这种大分子组装及其机制的许多基本问题仍未得到解答。
在当前结构数据的背景下，我们综述了A类GPCR亚家族与同源G蛋白复合物中界面和识别位点的结构细节，特别强调了激活对GPCR结构的影响、预组装GPCR/G蛋白复合物的普遍性、选择性偶联的关键结构决定因素以及GPCR寡聚化在此过程中的可能参与。
