Nature Communications (Aug 2020)

Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy

  • Jia Duan,
  • Dan-dan Shen,
  • X. Edward Zhou,
  • Peng Bi,
  • Qiu-feng Liu,
  • Yang-xia Tan,
  • You-wen Zhuang,
  • Hui-bing Zhang,
  • Pei-yu Xu,
  • Si-Jie Huang,
  • Shan-shan Ma,
  • Xin-heng He,
  • Karsten Melcher,
  • Yan Zhang,
  • H. Eric Xu,
  • Yi Jiang

DOI
https://doi.org/10.1038/s41467-020-17933-8
Journal volume & issue
Vol. 11, no. 1
pp. 1 – 10

Abstract

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Vasoactive intestinal polypeptide receptor (VIP1R) is a widely expressed class B G protein-coupled receptor and a drug target for the treatment of inflammatory diseases. Here authors report a cryoelectron microscopy structure of human VIP1R bound to PACAP27 and Gs heterotrimer, which provides insights into PACAP27 binding and VIP receptor activation.