Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy
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...
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Published in | Nature communications Vol. 11; no. 1; p. 4121 |
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Main Authors | , , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
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17.08.2020
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Abstract | 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 receptor is limited by the lack of structural information of VIP1R. Here we report a cryo-electron microscopy structure of human VIP1R bound to PACAP27 and Gs heterotrimer, whose complex assembly is stabilized by a NanoBiT tethering strategy. Comparison with other class B GPCR structures reveals that PACAP27 engages VIP1R with its N-terminus inserting into the ligand binding pocket at the transmembrane bundle of the receptor, which subsequently couples to the G protein in a receptor-specific manner. This structure has provided insights into the molecular basis of PACAP27 binding and VIP receptor activation. The methodology of the NanoBiT tethering may help to provide structural information of unstable complexes.
Vasoactive intestinal polypeptide receptor (VIP1R) is a widely expressed class B G protein-coupled receptor and a drug target for the treatment of inflammatory diseases. Here authors report a cryoelectron microscopy structure of human VIP1R bound to PACAP27 and Gs heterotrimer, which provides insights into PACAP27 binding and VIP receptor activation. |
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AbstractList | Vasoactive intestinal polypeptide receptor (VIP1R) is a widely expressed class B G protein-coupled receptor and a drug target for the treatment of inflammatory diseases. Here authors report a cryoelectron microscopy structure of human VIP1R bound to PACAP27 and Gs heterotrimer, which provides insights into PACAP27 binding and VIP receptor activation. 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 receptor is limited by the lack of structural information of VIP1R. Here we report a cryo-electron microscopy structure of human VIP1R bound to PACAP27 and Gs heterotrimer, whose complex assembly is stabilized by a NanoBiT tethering strategy. Comparison with other class B GPCR structures reveals that PACAP27 engages VIP1R with its N-terminus inserting into the ligand binding pocket at the transmembrane bundle of the receptor, which subsequently couples to the G protein in a receptor-specific manner. This structure has provided insights into the molecular basis of PACAP27 binding and VIP receptor activation. The methodology of the NanoBiT tethering may help to provide structural information of unstable complexes. 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 receptor is limited by the lack of structural information of VIP1R. Here we report a cryo-electron microscopy structure of human VIP1R bound to PACAP27 and Gs heterotrimer, whose complex assembly is stabilized by a NanoBiT tethering strategy. Comparison with other class B GPCR structures reveals that PACAP27 engages VIP1R with its N-terminus inserting into the ligand binding pocket at the transmembrane bundle of the receptor, which subsequently couples to the G protein in a receptor-specific manner. This structure has provided insights into the molecular basis of PACAP27 binding and VIP receptor activation. The methodology of the NanoBiT tethering may help to provide structural information of unstable complexes. Vasoactive intestinal polypeptide receptor (VIP1R) is a widely expressed class B G protein-coupled receptor and a drug target for the treatment of inflammatory diseases. Here authors report a cryoelectron microscopy structure of human VIP1R bound to PACAP27 and Gs heterotrimer, which provides insights into PACAP27 binding and VIP receptor activation. 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 receptor is limited by the lack of structural information of VIP1R. Here we report a cryo-electron microscopy structure of human VIP1R bound to PACAP27 and Gs heterotrimer, whose complex assembly is stabilized by a NanoBiT tethering strategy. Comparison with other class B GPCR structures reveals that PACAP27 engages VIP1R with its N-terminus inserting into the ligand binding pocket at the transmembrane bundle of the receptor, which subsequently couples to the G protein in a receptor-specific manner. This structure has provided insights into the molecular basis of PACAP27 binding and VIP receptor activation. The methodology of the NanoBiT tethering may help to provide structural information of unstable complexes.Vasoactive intestinal polypeptide receptor (VIP1R) is a widely expressed class B G protein-coupled receptor and a drug target for the treatment of inflammatory diseases. Here authors report a cryoelectron microscopy structure of human VIP1R bound to PACAP27 and Gs heterotrimer, which provides insights into PACAP27 binding and VIP receptor activation. |
ArticleNumber | 4121 |
Author | Liu, Qiu-feng Tan, Yang-xia Xu, Pei-yu He, Xin-heng Ma, Shan-shan Zhou, X. Edward Melcher, Karsten Shen, Dan-dan Xu, H. Eric Jiang, Yi Zhuang, You-wen Bi, Peng Huang, Si-Jie Duan, Jia Zhang, Hui-bing Zhang, Yan |
Author_xml | – sequence: 1 givenname: Jia surname: Duan fullname: Duan, Jia organization: The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences – sequence: 2 givenname: Dan-dan surname: Shen fullname: Shen, Dan-dan organization: Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Department of Biophysics, Zhejiang University School of Medicine – sequence: 3 givenname: X. Edward surname: Zhou fullname: Zhou, X. Edward organization: Center for Cancer and Cell Biology, Program for Structural Biology, Van Andel Institute – sequence: 4 givenname: Peng surname: Bi fullname: Bi, Peng organization: Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Department of Biophysics, Zhejiang University School of Medicine – sequence: 5 givenname: Qiu-feng surname: Liu fullname: Liu, Qiu-feng organization: The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences – sequence: 6 givenname: Yang-xia surname: Tan fullname: Tan, Yang-xia organization: The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences, School of Life Science and Technology, ShanghaiTech University – sequence: 7 givenname: You-wen surname: Zhuang fullname: Zhuang, You-wen organization: The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences – sequence: 8 givenname: Hui-bing surname: Zhang fullname: Zhang, Hui-bing organization: Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Department of Biophysics, Zhejiang University School of Medicine – sequence: 9 givenname: Pei-yu surname: Xu fullname: Xu, Pei-yu organization: The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences – sequence: 10 givenname: Si-Jie surname: Huang fullname: Huang, Si-Jie organization: The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences, School of Life Science and Technology, ShanghaiTech University – sequence: 11 givenname: Shan-shan surname: Ma fullname: Ma, Shan-shan organization: The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences – sequence: 12 givenname: Xin-heng orcidid: 0000-0001-7813-5480 surname: He fullname: He, Xin-heng organization: The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences – sequence: 13 givenname: Karsten orcidid: 0000-0002-9125-4027 surname: Melcher fullname: Melcher, Karsten organization: Center for Cancer and Cell Biology, Program for Structural Biology, Van Andel Institute – sequence: 14 givenname: Yan orcidid: 0000-0003-2189-0244 surname: Zhang fullname: Zhang, Yan email: zhang_yan@zju.edu.cn organization: Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Department of Biophysics, Zhejiang University School of Medicine – sequence: 15 givenname: H. Eric orcidid: 0000-0002-6829-8144 surname: Xu fullname: Xu, H. Eric email: eric.xu@simm.ac.cn organization: The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences, School of Life Science and Technology, ShanghaiTech University – sequence: 16 givenname: Yi orcidid: 0000-0002-0723-1413 surname: Jiang fullname: Jiang, Yi email: yijiang@simm.ac.cn organization: The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, University of Chinese Academy of Sciences |
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Snippet | Vasoactive intestinal polypeptide receptor (VIP1R) is a widely expressed class B G protein-coupled receptor and a drug target for the treatment of neuronal,... Vasoactive intestinal polypeptide receptor (VIP1R) is a widely expressed class B G protein-coupled receptor and a drug target for the treatment of inflammatory... |
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SourceType | Open Website Open Access Repository Aggregation Database Publisher |
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SubjectTerms | 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 |
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Title | Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy |
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