Heterotrimeric G protein β1γ2 subunits change orientation upon complex formation with G protein-coupled receptor kinase 2 (GRK2) on a model membrane
Heterotrimeric G protein β1γ2 subunits change orientation upon complex formation with G protein-coupled receptor kinase 2 (GRK2) on a model membrane
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DOI：
10.1073/pnas.1108236108
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发表时间：
2011-09-13
影响因子：
11.1
通讯作者：
Chen, Zhan
中科院分区：
文献类型：
--
作者：
Boughton, Andrew P.;Yang, Pei;Chen, Zhan
很少有实验技术可以评估外周膜蛋白在其天然环境中的方向。应用和频产生 (SFG) 振动光谱研究 G 蛋白偶联受体 (GPCR) 激酶 2 (GRK2) 和异三聚体 G 蛋白 beta(1)gamma(2) 亚基 (G beta gamma) 在脂质双层上形成的复合物，无需任何外源标记。 GRK2-G β γ 复合物最可能的膜方向与根据已知蛋白质晶体结构预测的方向不同，并且定位 GRK2 的预测受体对接位点，使其能够更佳地与 GPCR 相互作用。 G beta gamma 与 GRK2 结合后似乎也会改变其方向。所开发的方法广泛适用于其他膜蛋白的原位研究。
Few experimental techniques can assess the orientation of peripheral membrane proteins in their native environment. Sum Frequency Generation (SFG) vibrational spectroscopy was applied to study the formation of the complex between G protein-coupled receptor (GPCR) kinase 2 (GRK2) and heterotrimeric G protein beta(1)gamma(2) subunits (G beta gamma) at a lipid bilayer, without any exogenous labels. The most likely membrane orientation of the GRK2-G beta gamma complex differs from that predicted from the known protein crystal structure, and positions the predicted receptor docking site of GRK2 such that it would more optimally interact with GPCRs. G beta gamma also appears to change its orientation after binding to GRK2. The developed methodology is widely applicable for the study of other membrane proteins in situ.