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Crystal structures of agonist-bound human cannabinoid receptor CB1

Author

Listed:
  • Tian Hua

    (iHuman Institute, ShanghaiTech University
    National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Kiran Vemuri

    (Center for Drug Discovery, Department of Pharmaceutical Sciences
    Northeastern University)

  • Spyros P. Nikas

    (Center for Drug Discovery, Department of Pharmaceutical Sciences
    Northeastern University)

  • Robert B. Laprairie

    (The Scripps Research Institute)

  • Yiran Wu

    (iHuman Institute, ShanghaiTech University)

  • Lu Qu

    (iHuman Institute, ShanghaiTech University
    National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Mengchen Pu

    (iHuman Institute, ShanghaiTech University)

  • Anisha Korde

    (Center for Drug Discovery, Department of Pharmaceutical Sciences
    Northeastern University)

  • Shan Jiang

    (Center for Drug Discovery, Department of Pharmaceutical Sciences
    Northeastern University)

  • Jo-Hao Ho

    (The Scripps Research Institute)

  • Gye Won Han

    (Bridge Institute, University of Southern California)

  • Kang Ding

    (iHuman Institute, ShanghaiTech University
    University of Chinese Academy of Sciences
    School of Life Science and Technology, ShanghaiTech University)

  • Xuanxuan Li

    (Beijing Computational Science Research Center)

  • Haiguang Liu

    (Beijing Computational Science Research Center)

  • Michael A. Hanson

    (GPCR Consortium)

  • Suwen Zhao

    (iHuman Institute, ShanghaiTech University
    School of Life Science and Technology, ShanghaiTech University)

  • Laura M. Bohn

    (The Scripps Research Institute)

  • Alexandros Makriyannis

    (Center for Drug Discovery, Department of Pharmaceutical Sciences
    Northeastern University)

  • Raymond C. Stevens

    (iHuman Institute, ShanghaiTech University
    Bridge Institute, University of Southern California
    School of Life Science and Technology, ShanghaiTech University)

  • Zhi-Jie Liu

    (iHuman Institute, ShanghaiTech University
    National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
    School of Life Science and Technology, ShanghaiTech University)

Abstract

Crystal structures of the human cannabinoid receptor 1 (CB1) bound to the agonists AM11542 and AM841 reveal notable structural rearrangements upon receptor activation, and this flexibility may be a common feature among other G-protein-coupled receptors.

Suggested Citation

  • Tian Hua & Kiran Vemuri & Spyros P. Nikas & Robert B. Laprairie & Yiran Wu & Lu Qu & Mengchen Pu & Anisha Korde & Shan Jiang & Jo-Hao Ho & Gye Won Han & Kang Ding & Xuanxuan Li & Haiguang Liu & Michae, 2017. "Crystal structures of agonist-bound human cannabinoid receptor CB1," Nature, Nature, vol. 547(7664), pages 468-471, July.
    • Handle: RePEc:nat:nature:v:547:y:2017:i:7664:d:10.1038_nature23272
    DOI: 10.1038/nature23272
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    Citations

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    Cited by:

    1. Yang Yang & Hye Jin Kang & Ruogu Gao & Jingjing Wang & Gye Won Han & Jeffrey F. DiBerto & Lijie Wu & Jiahui Tong & Lu Qu & Yiran Wu & Ryan Pileski & Xuemei Li & Xuejun Cai Zhang & Suwen Zhao & Terry K, 2023. "Structural insights into the human niacin receptor HCA2-Gi signalling complex," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    2. Na Wang & Xinheng He & Jing Zhao & Hualiang Jiang & Xi Cheng & Yu Xia & H. Eric Xu & Yuanzheng He, 2022. "Structural basis of leukotriene B4 receptor 1 activation," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    3. Xuan Zhang & Guibing Liu & Ya-Ni Zhong & Ru Zhang & Chuan-Cheng Yang & Canyang Niu & Xuanyu Pu & Jingjing Sun & Tianyao Zhang & Lejin Yang & Chao Zhang & Xiu Li & Xinyuan Shen & Peng Xiao & Jin-Peng S, 2024. "Structural basis of ligand recognition and activation of the histamine receptor family," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    4. Susanne Prokop & Péter Ábrányi-Balogh & Benjámin Barti & Márton Vámosi & Miklós Zöldi & László Barna & Gabriella M. Urbán & András Dávid Tóth & Barna Dudok & Attila Egyed & Hui Deng & Gian Marco Leggi, 2021. "PharmacoSTORM nanoscale pharmacology reveals cariprazine binding on Islands of Calleja granule cells," Nature Communications, Nature, vol. 12(1), pages 1-19, December.
    5. Yuxia Qian & Jiening Wang & Linlin Yang & Yanru Liu & Lina Wang & Wei Liu & Yun Lin & Hong Yang & Lixin Ma & Sheng Ye & Shan Wu & Anna Qiao, 2022. "Activation and signaling mechanism revealed by GPR119-Gs complex structures," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    6. Xiaoting Li & Hao Chang & Jara Bouma & Laura V. Paus & Partha Mukhopadhyay & Janos Paloczi & Mohammed Mustafa & Cas Horst & Sanjay Sunil Kumar & Lijie Wu & Yanan Yu & Richard J. B. H. N. Berg & Antoni, 2023. "Structural basis of selective cannabinoid CB2 receptor activation," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    7. Kaavya Krishna Kumar & Michael J. Robertson & Elina Thadhani & Haoqing Wang & Carl-Mikael Suomivuori & Alexander S. Powers & Lipin Ji & Spyros P. Nikas & Ron O. Dror & Asuka Inoue & Alexandros Makriya, 2023. "Structural basis for activation of CB1 by an endocannabinoid analog," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    8. Hiroaki Akasaka & Tatsuki Tanaka & Fumiya K. Sano & Yuma Matsuzaki & Wataru Shihoya & Osamu Nureki, 2022. "Structure of the active Gi-coupled human lysophosphatidic acid receptor 1 complexed with a potent agonist," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    9. Elizaveta Lyapina & Egor Marin & Anastasiia Gusach & Philipp Orekhov & Andrey Gerasimov & Aleksandra Luginina & Daniil Vakhrameev & Margarita Ergasheva & Margarita Kovaleva & Georgii Khusainov & Polin, 2022. "Structural basis for receptor selectivity and inverse agonism in S1P5 receptors," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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