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Ligand recognition and allosteric regulation of DRD1-Gs signaling complexes.

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作者：
Peng Xiao[1,2] ; Wei Yan[1] ; Lu Gou[3] ; Ya-Ni Zhong[2] ; Liangliang Kong[5] ; Chao Wu[1] ; Xin Wen[2] ; Yuan Yuan[1] ; Sheng Cao[7] ; Changxiu Qu[2] ; Xin Yang[1] ; Chuan-Cheng Yang[2] ; Anjie Xia[1] ; Zhenquan Hu[10] ; Qianqian Zhang[11] ; Yong-Hao He[2,12] ; Dao-Lai Zhang[12] ; Chao Zhang[9] ; Gui-Hua Hou[9] ; Huanxiang Liu[11] ; Lizhe Zhu[10] ; Ping Fu[1] ; Shengyong Yang[1] ; Daniel M. Rosenbaum[8] ; Jin-Peng Sun[2,6] ; Yang Du[7] ; Lei Zhang[3] ; Xiao Yu[4] ; Zhenhua Shao[1] ;
机构： [1]Division of Nephrology and Kidney Research Institute, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, SichuanUniversity, Chengdu, Sichuan 610041, China [2]Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School ofBasic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, Shandong 250012, China [3]MOE Key Laboratory for Nonequilibrium Synthesis and Modulation of Condensed Matter, School of Physics, Xi’an Jiaotong University, Xi’an710049, China [4]Key Laboratory Experimental Teratology of the Ministry of Education and Department of Physiology, School of Basic Medical Sciences,Cheeloo College of Medicine, Shandong University, Jinan, Shandong 250012, China [5]National Facility for Protein Science in Shanghai, Zhangjiang Lab, Shanghai Advanced Research Institute, Chinese Academy of Sciences,Shanghai 201204, China [6]Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Peking University, Key Laboratory of MolecularCardiovascular Science, Ministry of Education, Beijing 100191, China [7]School of Life and Health Sciences, Kobilka Institute of Innovative Drug Discovery, Chinese University of Hong Kong, Shenzhen, Guangdong518172, China [8]Department of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX 75390, USA [9]Biomedical Isotope Research Center, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan,Shandong 250012, China [10]Warshel Institute for Computational Biology, The Chinese University of Hong Kong, Shenzhen, Guangdong 518172, China [11]School of Pharmacy, Lanzhou University, Lanzhou 730000, China [12]School of Pharmacy, Binzhou Medical University, Yantai, Shandong 264003, China
出处：
DOI： 10.1016/j.cell.2021.01.028
ISSN：

摘要：
Dopamine receptors, including D1- and D2-like receptors, are important therapeutic targets in a variety of neurological syndromes, as well as cardiovascular and kidney diseases. Here, we present five cryoelectron microscopy (cryo-EM) structures of the dopamine D1 receptor (DRD1) coupled to Gs heterotrimer in complex with three catechol-based agonists, a non-catechol agonist, and a positive allosteric modulator for endogenous dopamine. These structures revealed that a polar interaction network is essential for catecholamine-like agonist recognition, whereas specific motifs in the extended binding pocket were responsible for discriminating D1- from D2-like receptors. Moreover, allosteric binding at a distinct inner surface pocket improved the activity of DRD1 by stabilizing endogenous dopamine interaction at the orthosteric site. DRD1-Gs interface revealed key features that serve as determinants for G protein coupling. Together, our study provides a structural understanding of the ligand recognition, allosteric regulation, and G protein coupling mechanisms of DRD1. Copyright © 2021 Elsevier Inc. All rights reserved.

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出版当年[2021]版：
大类 | 1 区 生物学
小类 | 1 区 生化与分子生物学 1 区 细胞生物学
最新[2023]版：
大类 | 1 区 生物学
小类 | 1 区 生化与分子生物学 1 区 细胞生物学
第一作者：
第一作者机构： [1]Division of Nephrology and Kidney Research Institute, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, SichuanUniversity, Chengdu, Sichuan 610041, China [2]Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School ofBasic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, Shandong 250012, China
共同第一作者：
通讯作者：
通讯机构： [2]Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School ofBasic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, Shandong 250012, China [6]Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Peking University, Key Laboratory of MolecularCardiovascular Science, Ministry of Education, Beijing 100191, China
推荐引用方式(GB/T 7714)：
Peng Xiao,Wei Yan,Lu Gou,et al.Ligand recognition and allosteric regulation of DRD1-Gs signaling complexes.[J].Cell.2021,184(4):943-956.e18.doi:10.1016/j.cell.2021.01.028.
APA：
Peng Xiao,Wei Yan,Lu Gou,Ya-Ni Zhong,Liangliang Kong...&Zhenhua Shao.(2021).Ligand recognition and allosteric regulation of DRD1-Gs signaling complexes..Cell,184,(4)
MLA：
Peng Xiao,et al."Ligand recognition and allosteric regulation of DRD1-Gs signaling complexes.".Cell 184..4(2021):943-956.e18

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