Recent Progress in Understanding the Conformational Mechanism of Heterotrimeric G Protein Activation.
10.4062/biomolther.2016.169
- Author:
Nguyen Minh DUC
1
;
Hee Ryung KIM
;
Ka Young CHUNG
Author Information
1. School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea. kychung2@skku.edu
- Publication Type:Review
- Keywords:
G protein;
G protein-coupled receptor;
Structure;
Dynamics
- MeSH:
GTP-Binding Proteins*;
Heterotrimeric GTP-Binding Proteins
- From:Biomolecules & Therapeutics
2017;25(1):4-11
- CountryRepublic of Korea
- Language:English
-
Abstract:
Heterotrimeric G proteins are key intracellular coordinators that receive signals from cells through activation of cognate G protein-coupled receptors (GPCRs). The details of their atomic interactions and structural mechanisms have been described by many biochemical and biophysical studies. Specifically, a framework for understanding conformational changes in the receptor upon ligand binding and associated G protein activation was provided by description of the crystal structure of the β2-adrenoceptor-Gs complex in 2011. This review focused on recent findings in the conformational dynamics of G proteins and GPCRs during activation processes.
