首页> 美国卫生研究院文献>Proceedings of the National Academy of Sciences of the United States of America >PNAS Plus: 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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PNAS Plus: Heterotrimeric G protein β1γ2 subunits change orientation upon complex formation with G protein-coupled receptor kinase 2 (GRK2) on a model membrane

机译:PNAS Plus:异源三聚体G蛋白β1γ2亚基在模型膜上与G蛋白偶联受体激酶2(GRK2)形成复合物后会改变方向

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摘要

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 β1γ2 subunits (Gβγ) at a lipid bilayer, without any exogenous labels. The most likely membrane orientation of the GRK2-Gβγ 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. Gβγ 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.
机译:很少有实验技术可以评估其天然环境中外周膜蛋白的方向。应用总频率生成(SFG)振动光谱法研究了在脂质双层中G蛋白偶联受体(GPCR)激酶2(GRK2)和异三聚G蛋白β1γ2亚基(Gβγ)之间没有任何外源标记的复合物的形成。 GRK2-Gβγ复合物最可能的膜取向与已知蛋白质晶体结构所预测的不同,并且将所预测的GRK2受体对接位点定位,从而使其与GPCR相互作用更佳。 Gβγ与GRK2结合后也似乎改变了其方向。所开发的方法可广泛用于其他原位膜蛋白的研究。

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