Structures of signaling complexes of lipid receptors S1PR1 and S1PR5 reveal mechanisms of activation and drug recognition
Sphingosine-1-phosphate (S1P) is an important bioactive lipid molecule in cell membrane metabolism and binds to G protein-coupled S1P receptors (S1PRs) to regulate embryonic development, physiological homeostasis, and pathogenic processes in various organs. S1PRs are lipid-sensing receptors and are...
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| Veröffentlicht in: | Cell research 2021-12, Vol.31 (12), p.1263-1274 |
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| container_title | Cell research |
| container_volume | 31 |
| creator | Yuan, Yuan Jia, Guowen Wu, Chao Wang, Wei Cheng, Lin Li, Qian Li, Ziyan Luo, Kaidong Yang, Shengyong Yan, Wei Su, Zhaoming Shao, Zhenhua |
| description | Sphingosine-1-phosphate (S1P) is an important bioactive lipid molecule in cell membrane metabolism and binds to G protein-coupled S1P receptors (S1PRs) to regulate embryonic development, physiological homeostasis, and pathogenic processes in various organs. S1PRs are lipid-sensing receptors and are therapeutic targets for drug development, including potential treatment of COVID-19. Herein, we present five cryo-electron microscopy structures of S1PRs bound to diverse drug agonists and the heterotrimeric Gi protein. Our structural and functional assays demonstrate the different binding modes of chemically distinct agonists of S1PRs, reveal the mechanical switch that activates these receptors, and provide a framework for understanding ligand selectivity and G protein coupling. |
| doi_str_mv | 10.1038/s41422-021-00566-x |
| format | Article |
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S1PRs are lipid-sensing receptors and are therapeutic targets for drug development, including potential treatment of COVID-19. Herein, we present five cryo-electron microscopy structures of S1PRs bound to diverse drug agonists and the heterotrimeric Gi protein. Our structural and functional assays demonstrate the different binding modes of chemically distinct agonists of S1PRs, reveal the mechanical switch that activates these receptors, and provide a framework for understanding ligand selectivity and G protein coupling.</description><identifier>ISSN: 1001-0602</identifier><identifier>EISSN: 1748-7838</identifier><identifier>DOI: 10.1038/s41422-021-00566-x</identifier><identifier>PMID: 34526663</identifier><language>eng</language><publisher>Singapore: Springer Singapore</publisher><subject>101/28 ; 631/535/1258/1259 ; 631/80/86/2365 ; 96/95 ; Agonists ; Azetidines - chemistry ; Azetidines - metabolism ; Benzyl Compounds - chemistry ; Benzyl Compounds - metabolism ; Biomedical and Life Sciences ; Cell Biology ; Cell membranes ; COVID-19 ; Cryoelectron Microscopy ; Drug development ; Electron microscopy ; Embryogenesis ; Embryonic growth stage ; G protein-coupled receptors ; Homeostasis ; Humans ; Life Sciences ; Lipids ; Molecular Dynamics Simulation ; Organs ; Protein Binding ; Protein Structure, Quaternary ; Protein turnover ; Proteins ; Receptors ; Selectivity ; Signal Transduction ; Sphingosine 1-phosphate ; Sphingosine-1-Phosphate Receptors - agonists ; Sphingosine-1-Phosphate Receptors - genetics ; Sphingosine-1-Phosphate Receptors - metabolism ; Structure-function relationships ; Therapeutic targets</subject><ispartof>Cell research, 2021-12, Vol.31 (12), p.1263-1274</ispartof><rights>The Author(s), under exclusive licence to Center for Excellence in Molecular Cell Science, CAS 2021</rights><rights>2021. 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S1PRs are lipid-sensing receptors and are therapeutic targets for drug development, including potential treatment of COVID-19. Herein, we present five cryo-electron microscopy structures of S1PRs bound to diverse drug agonists and the heterotrimeric Gi protein. Our structural and functional assays demonstrate the different binding modes of chemically distinct agonists of S1PRs, reveal the mechanical switch that activates these receptors, and provide a framework for understanding ligand selectivity and G protein coupling.</description><subject>101/28</subject><subject>631/535/1258/1259</subject><subject>631/80/86/2365</subject><subject>96/95</subject><subject>Agonists</subject><subject>Azetidines - chemistry</subject><subject>Azetidines - metabolism</subject><subject>Benzyl Compounds - chemistry</subject><subject>Benzyl Compounds - metabolism</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Biology</subject><subject>Cell membranes</subject><subject>COVID-19</subject><subject>Cryoelectron Microscopy</subject><subject>Drug development</subject><subject>Electron microscopy</subject><subject>Embryogenesis</subject><subject>Embryonic growth stage</subject><subject>G protein-coupled receptors</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Lipids</subject><subject>Molecular Dynamics Simulation</subject><subject>Organs</subject><subject>Protein Binding</subject><subject>Protein Structure, Quaternary</subject><subject>Protein turnover</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Selectivity</subject><subject>Signal Transduction</subject><subject>Sphingosine 1-phosphate</subject><subject>Sphingosine-1-Phosphate Receptors - 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S1PRs are lipid-sensing receptors and are therapeutic targets for drug development, including potential treatment of COVID-19. Herein, we present five cryo-electron microscopy structures of S1PRs bound to diverse drug agonists and the heterotrimeric Gi protein. Our structural and functional assays demonstrate the different binding modes of chemically distinct agonists of S1PRs, reveal the mechanical switch that activates these receptors, and provide a framework for understanding ligand selectivity and G protein coupling.</abstract><cop>Singapore</cop><pub>Springer Singapore</pub><pmid>34526663</pmid><doi>10.1038/s41422-021-00566-x</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0001-7204-801X</orcidid><orcidid>https://orcid.org/0000-0002-9279-1721</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 101/28 631/535/1258/1259 631/80/86/2365 96/95 Agonists Azetidines - chemistry Azetidines - metabolism Benzyl Compounds - chemistry Benzyl Compounds - metabolism Biomedical and Life Sciences Cell Biology Cell membranes COVID-19 Cryoelectron Microscopy Drug development Electron microscopy Embryogenesis Embryonic growth stage G protein-coupled receptors Homeostasis Humans Life Sciences Lipids Molecular Dynamics Simulation Organs Protein Binding Protein Structure, Quaternary Protein turnover Proteins Receptors Selectivity Signal Transduction Sphingosine 1-phosphate Sphingosine-1-Phosphate Receptors - agonists Sphingosine-1-Phosphate Receptors - genetics Sphingosine-1-Phosphate Receptors - metabolism Structure-function relationships Therapeutic targets |
| title | Structures of signaling complexes of lipid receptors S1PR1 and S1PR5 reveal mechanisms of activation and drug recognition |
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