Activation of G-protein Galpha subunits by receptors through Galpha-Gbeta and Galpha-Ggamma interactions.
Activation of G-protein Galpha subunits by receptors through Galpha-Gbeta and Galpha-Ggamma interactions.
复制标题
受体通过 Galpha-Gbeta 和 Galpha-Ggamma 相互作用激活 G 蛋白 Galpha 亚基。
DOI：
--
复制
发表时间：
2003
期刊：
影响因子：
--
通讯作者：
M. Chabre
中科院分区：
文献类型：
--
作者：
J. Cherfils;M. Chabre
跨膜受体激活异三聚体 GTP 结合蛋白的 Gα 亚基需要将结构信号从受体结合位点传播到蛋白质另一侧的核苷酸结合位点。在之前的模型中，有人认为 Gbeta-Ggamma 二聚体通过 Galpha N 端螺旋的杠杆臂运动倾斜远离 Galpha。在这里，我们提出运动发生在相反的方向，紧密堆积 Galpha-Gbeta 界面，并在 Galpha 的螺旋域和 Ggamma 的 N 末端之间创建一个新颖的界面，这决定了激活的特异性。
Activation of the Galpha subunit of heterotrimeric GTP-binding proteins by transmembrane receptors requires the propagation of structural signals from the receptor-binding site to the nucleotide-binding site at the opposite side of the protein. In a previous model, it was suggested that the Gbeta-Ggamma dimer is tilted away from Galpha by a lever-arm motion of the Galpha N-terminal helix. Here, we propose that the motion occurs in the opposite direction, close-packing the Galpha-Gbeta interface and creating a novel interface between the helical domain of Galpha and the N terminus of Ggamma, which determines the specificity of activation.