Structure insights into selective coupling of G protein subtypes by a class B G protein-coupled receptor

Li-Hua Zhao (), Jingyu Lin, Su-Yu Ji, X. Edward Zhou, Chunyou Mao, Dan-Dan Shen, Xinheng He, Peng Xiao, Jinpeng Sun, Karsten Melcher, Yan Zhang (), Xiao Yu () and H. Eric Xu ()
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Li-Hua Zhao: Chinese Academy of Sciences
Jingyu Lin: Shandong University
Su-Yu Ji: Zhejiang University School of Medicine
X. Edward Zhou: Van Andel Research Institute
Chunyou Mao: Zhejiang University School of Medicine
Dan-Dan Shen: Zhejiang University School of Medicine
Xinheng He: Chinese Academy of Sciences
Peng Xiao: Shandong University
Jinpeng Sun: Shandong University
Karsten Melcher: Van Andel Research Institute
Yan Zhang: Zhejiang University School of Medicine
Xiao Yu: Shandong University
H. Eric Xu: Chinese Academy of Sciences

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: Abstract The ability to couple with multiple G protein subtypes, such as Gs, Gi/o, or Gq/11, by a given G protein-coupled receptor (GPCR) is critical for many physiological processes. Over the past few years, the cryo-EM structures for all 15 members of the medically important class B GPCRs, all in complex with Gs protein, have been determined. However, no structure of class B GPCRs with Gq/11 has been solved to date, limiting our understanding of the precise mechanisms of G protein coupling selectivity. Here we report the structures of corticotropin releasing factor receptor 2 (CRF2R) bound to Urocortin 1 (UCN1), coupled with different classes of heterotrimeric G proteins, G11 and Go. We compare these structures with the structure of CRF2R in complex with Gs to uncover the structural differences that determine the selective coupling of G protein subtypes by CRF2R. These results provide important insights into the structural basis for the ability of CRF2R to couple with multiple G protein subtypes.

Date: 2022
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DOI: 10.1038/s41467-022-33851-3

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