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

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

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 insigh...

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Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/00cdfea6e7c6478cbc6a497c3496d163
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Sumario: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.

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