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

• Published in: Nature communications Vol. 11; no. 1; p. 4121
• Main Authors: Duan, Jia, Shen, Dan-dan, Zhou, X. Edward, Bi, Peng, Liu, Qiu-feng, Tan, Yang-xia, Zhuang, You-wen, Zhang, Hui-bing, Xu, Pei-yu, Huang, Si-Jie, Ma, Shan-shan, He, Xin-heng, Melcher, Karsten, Zhang, Yan, Xu, H. Eric, Jiang, Yi
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 17.08.2020; Nature Publishing Group; Nature Portfolio
• Subjects: 101/28; 631/45/612/194; 631/535/1258/1259; Activation; Binding; Electron microscopy; G protein-coupled receptors; Humanities and Social Sciences; Inflammatory diseases; Intestine; Medical treatment; Microscopy; Molecular structure; multidisciplinary; N-Terminus; Polypeptides; Proteins; Receptor mechanisms; Receptors; Science; Science (multidisciplinary); Tethering; Therapeutic targets; Vasoactive agents; Vasoactive intestinal peptide

Vasoactive intestinal polypeptide receptor (VIP1R) is a widely expressed class B G protein-coupled receptor and a drug target for the treatment of neuronal, metabolic, and inflammatory diseases. However, our understanding of its mechanism of action and the potential of drug discovery targeting this...