Ligand recognition and allosteric regulation of DRD1-Gs signaling complexes

Peng Xiao, Wei Yan, Lu Gou, Ya Ni Zhong, Liangliang Kong, Chao Wu, Xin Wen, Yuan Yuan, Sheng Cao, Changxiu Qu, Xin Yang, Chuan Cheng Yang, Anjie Xia, Zhenquan Hu, Qianqian Zhang, Yong Hao He, Dao Lai Zhang, Chao Zhang, Gui Hua Hou, Huanxiang LiuLizhe Zhu, Ping Fu, Shengyong Yang, Daniel M. Rosenbaum, Jin Peng Sun, Yang Du, Lei Zhang, Xiao Yu, Zhenhua Shao

Research output: Contribution to journalArticlepeer-review

Abstract

The cryo-EM structures of DRD1 coupled to its G protein, in complex with important agonists, elucidates the mechanism of G-protein-coupled selectivity and will facilitate future drug discovery and design.

Original languageEnglish (US)
Pages (from-to)943-956.e18
JournalCell
Volume184
Issue number4
DOIs
StatePublished - Feb 18 2021

Keywords

  • DRD1-Gs complex
  • allosteric regulation
  • catecholamine
  • ccryo-EM
  • dopamine receptor
  • noncatechol
  • positive allosteric modulator
  • structure

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Fingerprint

Dive into the research topics of 'Ligand recognition and allosteric regulation of DRD1-Gs signaling complexes'. Together they form a unique fingerprint.

Cite this