异源三聚体G蛋白的2.0埃晶体结构。
The 2.0 A crystal structure of a heterotrimeric G protein.
作者信息
Lambright D G, Sondek J, Bohm A, Skiba N P, Hamm H E, Sigler P B
机构信息
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA.
出版信息
Nature. 1996 Jan 25;379(6563):311-9. doi: 10.1038/379311a0.
The structure of a heterotrimeric G protein reveals the mechanism of the nucleotide-dependent engagement of the alpha and beta gamma subunits that regulates their interaction with receptor and effector molecules. The interaction involves two distinct interfaces and dramatically alters the conformation of the alpha but not of the beta gamma subunits. The location of the known sites for post-translational modification and receptor coupling suggest a plausible orientation with respect to the membrane surface and an activated heptahelical receptor.
异源三聚体G蛋白的结构揭示了α亚基和βγ亚基核苷酸依赖性结合的机制，这种结合调节了它们与受体及效应分子的相互作用。这种相互作用涉及两个不同的界面，并且极大地改变了α亚基的构象，但未改变βγ亚基的构象。已知的翻译后修饰位点和受体偶联位点的位置表明了其相对于膜表面和活化的七螺旋受体的合理取向。
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