中文版 | English
Title

Structures of the ADGRG2-G(s) complex in apo and ligand-bound forms

Author
Corresponding AuthorYi, Fan; Liu, Zhongmin; Sun, Jin-Peng; Yu, Xiao
Publication Years
2022-08-01
DOI
Source Title
ISSN
1552-4450
EISSN
1552-4469
Abstract
Adhesion G protein-coupled receptors are elusive in terms of their structural information and ligands. Here, we solved the cryogenic-electron microscopy (cryo-EM) structure of apo-ADGRG2, an essential membrane receptor for maintaining male fertility, in complex with a G(s) trimer. Whereas the formations of two kinks were determinants of the active state, identification of a potential ligand-binding pocket in ADGRG2 facilitated the screening and identification of dehydroepiandrosterone (DHEA), dehydroepiandrosterone sulfate and deoxycorticosterone as potential ligands of ADGRG2. The cryo-EM structures of DHEA-ADGRG2-G(s) provided interaction details for DHEA within the seven transmembrane domains of ADGRG2. Collectively, our data provide a structural basis for the activation and signaling of ADGRG2, as well as characterization of steroid hormones as ADGRG2 ligands, which might be used as useful tools for further functional studies of the orphan ADGRG2.
URL[Source Record]
Indexed By
Language
English
Important Publications
NI Journal Papers
SUSTech Authorship
Corresponding
Funding Project
National Key R&D Program of China["2018YFC1003600","2019YFA0904200"] ; National Natural Science Foundation of China["92057121","31971195","82090024","91949202","32000850"] ; National Science Fund for Distinguished Young Scholars[81825022] ; Major Fundamental Research Program of Natural Science Foundation of Shandong Province, China["ZR2021ZD18","ZR2020ZD39"] ; Shandong Provincial Natural Science Fund for Excellent Young Scholars[ZR2021YQ18] ; Key Research and Development Program of Shandong Province["2021ZLGX02","GG201709260059"] ; Key Research Project of the Natural Science Foundation of Beijing, China[Z20J00129] ; Rolling program of ChangJiang Scholars and Innovative Research Team in University[IRT_17R68] ; Fundamental Research Funds for the Central Universities[2021JCG020]
WOS Research Area
Biochemistry & Molecular Biology
WOS Subject
Biochemistry & Molecular Biology
WOS Accession No
WOS:000842209100001
Publisher
Data Source
Web of Science
Citation statistics
Cited Times [WOS]:0
Document TypeJournal Article
Identifierhttp://kc.sustech.edu.cn/handle/2SGJ60CL/382586
DepartmentDepartment of Biology
Affiliation
1.Shandong Univ, Cheeloo Coll Med, Sch Basic Med Sci, Dept Physiol,Key Lab Expt Teratol,Minist Educ, Jinan, Peoples R China
2.Shandong Univ, Hosp 2, Dept Clin Lab, Jinan, Peoples R China
3.Shandong Univ, Cheeloo Coll Med, Adv Med Res Inst, Jinan, Peoples R China
4.Shandong Univ, Cheeloo Coll Med, Dept Biochem & Mol Biol, Sch Basic Med Sci,Key Lab Expt Teratol,Minist Edu, Jinan, Peoples R China
5.Peking Univ, Sch Basic Med Sci, Dept Physiol & Pathophysiol, Key Lab Mol Cardiovasc Sci,Minist Educ, Beijing, Peoples R China
6.Southern Univ Sci & Technol, Dept Biol, Shenzhen, Peoples R China
7.Tsinghua Univ, Sch Med, Beijing, Peoples R China
8.Univ Sci & Technol China, Sch Life Sci, Hefei, Peoples R China
9.Shandong Univ, Cheeloo Coll Med, Ctr Reprod Med, Jinan, Peoples R China
10.Binzhou Med Univ, Sch Pharm, Yantai, Peoples R China
11.Nantong Univ, Sch Med, Inst Reprod Med, Nantong, Peoples R China
12.Natl Hlth & Family Planning Commiss, Key Lab Male Reprod Hlth, Natl Res Inst Family Planning, Beijing, Peoples R China
13.Peking Univ Third Hosp, Dept Urol, Beijing, Peoples R China
14.Sichuan Univ, West China Univ Hosp 2, Dept Obstet Gynecol,Minist Educ, Joint Lab Reprod Med SCU CUHK,Key Lab Obstetr Gyn, Chengdu, Peoples R China
15.Shandong Univ, Sch Basic Med Sci, Dept Pharmacol, Key Lab Infect & Immun Shandong Prov, Jinan, Peoples R China
Recommended Citation
GB/T 7714
Lin, Hui,Xiao, Peng,Bu, Rui-Qian,et al. Structures of the ADGRG2-G(s) complex in apo and ligand-bound forms[J]. Nature Chemical Biology,2022.
APA
Lin, Hui.,Xiao, Peng.,Bu, Rui-Qian.,Guo, Shengchao.,Yang, Zhao.,...&Yu, Xiao.(2022).Structures of the ADGRG2-G(s) complex in apo and ligand-bound forms.Nature Chemical Biology.
MLA
Lin, Hui,et al."Structures of the ADGRG2-G(s) complex in apo and ligand-bound forms".Nature Chemical Biology (2022).
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