Structural Aspects of GPCR-G Protein Coupling.
- Author:
Ka Young CHUNG
1
Author Information
1. School of Pharmacy, Sungkyunkwan University, Suwon, Korea. kychung2@skku.edu
- Publication Type:Review
- Keywords:
GPCR;
G protein;
Structure
- MeSH:
GTP-Binding Proteins;
Guanosine Diphosphate;
Heterotrimeric GTP-Binding Proteins;
Membranes;
Signal Transduction
- From:Toxicological Research
2013;29(3):149-155
- CountryRepublic of Korea
- Language:English
-
Abstract:
G protein-coupled receptors (GPCRs) are membrane receptors; approximately 40% of drugs on the market target GPCRs. A precise understanding of the activation mechanism of GPCRs would facilitate the development of more effective and less toxic drugs. Heterotrimeric G proteins are important molecular switches in GPCR-mediated signal transduction. An agonist-activated receptor interacts with specific sites on G proteins and promotes the release of GDP from the Galpha subunit. Because of the important biological role of the GPCR-G protein coupling, conformational changes in the G protein upon receptor coupling have been of great interest. One of the most important questions was the interface between the GPCR and G proteins and the structural mechanism of GPCR-induced G protein activation. A number of biochemical and biophysical studies have been performed since the late 80s to address these questions; there was a significant breakthrough in 2011 when the crystal structure of a GPCR-G protein complex was solved. This review discusses the structural aspects of GPCR-G protein coupling by comparing the results of previous biochemical and biophysical studies to the GPCR-G protein crystal structure.
