Your browser doesn't support javascript.
loading
Structures of the ADGRG2-Gs complex in apo and ligand-bound forms.
Lin, Hui; Xiao, Peng; Bu, Rui-Qian; Guo, Shengchao; Yang, Zhao; Yuan, Daopeng; Zhu, Zhong-Liang; Zhang, Chuan-Xin; He, Qing-Tao; Zhang, Chao; Ping, Yu-Qi; Zhao, Ru-Jia; Ma, Chuan-Shun; Liu, Chang-Hao; Zhang, Xiao-Ning; Jiang, Dan; Huang, Shaohui; Xi, Yue-Tong; Zhang, Dao-Lai; Xue, Chen-Yang; Yang, Bai-Sheng; Li, Jian-Yuan; Lin, Hao-Cheng; Zeng, Xu-Hui; Zhao, Han; Xu, Wen-Ming; Yi, Fan; Liu, Zhongmin; Sun, Jin-Peng; Yu, Xiao.
Afiliación
  • Lin H; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Physiology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Xiao P; Department of Clinical Laboratory, The Second Hospital, and Advanced Medical Research Institute, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Bu RQ; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Guo S; Key Laboratory of Molecular Cardiovascular Science of the Ministry of Education, Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Peking University, Beijing, China.
  • Yang Z; Department of Clinical Laboratory, The Second Hospital, and Advanced Medical Research Institute, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Yuan D; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Zhu ZL; Department of Biology, Southern University of Science and Technology, Shenzhen, China.
  • Zhang CX; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • He QT; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Physiology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Zhang C; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Ping YQ; School of Medicine, Tsinghua University, Beijing, China.
  • Zhao RJ; School of Life Sciences, University of Science and Technology of China, Hefei, China.
  • Ma CS; Center for Reproductive Medicine, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Liu CH; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Zhang XN; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Jiang D; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Huang S; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Xi YT; School of Pharmacy, Binzhou Medical University, Yantai, China.
  • Zhang DL; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Physiology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Xue CY; Institute of Reproductive Medicine, School of Medicine, Nantong University, Nantong, China.
  • Yang BS; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Li JY; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Physiology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Lin HC; Key Laboratory of Experimental Teratology of the Ministry of Education, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, China.
  • Zeng XH; School of Pharmacy, Binzhou Medical University, Yantai, China.
  • Zhao H; Department of Biology, Southern University of Science and Technology, Shenzhen, China.
  • Xu WM; Department of Biology, Southern University of Science and Technology, Shenzhen, China.
  • Yi F; Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning, National Health and Family Planning Commission, Beijing, China.
  • Liu Z; Department of Urology, Peking University Third Hospital, Beijing, China.
  • Sun JP; Institute of Reproductive Medicine, School of Medicine, Nantong University, Nantong, China.
  • Yu X; Center for Reproductive Medicine, Cheeloo College of Medicine, Shandong University, Jinan, China.
Nat Chem Biol ; 18(11): 1196-1203, 2022 Nov.
Article en En | MEDLINE | ID: mdl-35982227
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 Gs 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-Gs 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.
Asunto(s)
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transducción de Señal / Receptores Acoplados a Proteínas G Límite: Humans / Male Idioma: En Revista: Nat Chem Biol Asunto de la revista: BIOLOGIA / QUIMICA Año: 2022 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transducción de Señal / Receptores Acoplados a Proteínas G Límite: Humans / Male Idioma: En Revista: Nat Chem Biol Asunto de la revista: BIOLOGIA / QUIMICA Año: 2022 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos