Backbone resonance assignments for G protein α(i3) subunit in the GTP-bound state
Backbone resonance assignments for G protein α(i3) subunit in the GTP-bound state
复制标题
G 蛋白 α(i3) 亚基在 GTP 结合状态下的骨架共振分配
DOI:
10.1007/s12104-012-9361-6
复制
发表时间:
2012
影响因子:
0.9
通讯作者:
Shimada I.
中科院分区:
文献类型:
--
作者:
Mase Y;Yokogawa M;Osawa M;Shimada I.
Guanine-nucleotide binding proteins (G proteins) act as molecular switches in signaling pathways, by coupling the activation of G protein-coupled receptors (GPCRs) at the cell surface to intracellular responses. In the resting state, G protein forms a heterotrimer, consisting of GDP-bound form of the G protein α subunit (Gα(GDP)) and G protein βγ subunit (Gβγ). Ligand binding to GPCRs promotes the GDP-GTP exchange on Gα, leading to the dissociation of the GTP-bound form of Gα (Gα(GTP)) and Gβγ. Then, Gα(GTP) and Gβγ bind to their downstream effector enzymes or ion channels and regulate their activities, leading to a variety of cellular responses. Finally, Gα hydrolyzes the bound GTP to GDP and returns to the resting state by re-associating with Gβγ. G proteins are classified with four major families based on the amino acid sequences of Gα: i/o, s, q/11, and 12/13. Each family transduces the signaling from different GPCRs to the specific effectors. Here, we established the backbone resonance assignments of human Gαi3, a member of the i/o family, with a molecular weight of 41 K in complex with a GTP analogue, GTPγS.