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
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/00cdfea6e7c6478cbc6a497c3496d163
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spelling	oai:doaj.org-article:00cdfea6e7c6478cbc6a497c3496d1632021-12-02T16:46:37ZCryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy10.1038/s41467-020-17933-82041-1723https://doaj.org/article/00cdfea6e7c6478cbc6a497c3496d1632020-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17933-8https://doaj.org/toc/2041-1723Vasoactive 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.Jia DuanDan-dan ShenX. Edward ZhouPeng BiQiu-feng LiuYang-xia TanYou-wen ZhuangHui-bing ZhangPei-yu XuSi-Jie HuangShan-shan MaXin-heng HeKarsten MelcherYan ZhangH. Eric XuYi JiangNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy
description	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.
format	article
author	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
author_facet	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
author_sort	Jia Duan
title	Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy
title_short	Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy
title_full	Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy
title_fullStr	Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy
title_full_unstemmed	Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy
title_sort	cryo-em structure of an activated vip1 receptor-g protein complex revealed by a nanobit tethering strategy
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/00cdfea6e7c6478cbc6a497c3496d163
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Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy

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