变构调节
G蛋白偶联受体
跨膜结构域
化学
二聚体
受体
生物化学
生物物理学
生物
有机化学
作者
Soo‐Kyung Kim,Yalu Chen,Ravinder Abrol,William A. Goddard,Brian Güthrie
标识
DOI:10.1073/pnas.1700001114
摘要
Significance We report a dynamical study of sweet receptor heterodimer, for which there are abundant data for various sweeteners. Because there is no crystal structure of a complete G protein-coupled receptor (GPCR) dimer of class C, we predicted the three-dimensional structure and carried out molecular dynamics with and without the sweetener agonists. We found that binding the sweetener induces major conformational changes during which the transmembrane domain (TMD) transforms from the TMD 56 interface to the TMD 6 interface, which is consistent with biophysical studies on activation of metabotropic glutamate receptor 2 homodimers, also class C. These results provide insights for how GPCRs are activated, which may have a major impact on understanding activation of other GPCR therapeutic targets.
科研通智能强力驱动
Strongly Powered by AbleSci AI