Crystal structures of agonist-bound human cannabinoid receptor CB1

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, Michael A. Hanson, Suwen Zhao (), Laura M. Bohn (), Alexandros Makriyannis (), Raymond C. Stevens and Zhi-Jie Liu ()
Additional contact information
Tian Hua: iHuman Institute, ShanghaiTech University
Kiran Vemuri: Center for Drug Discovery, Department of Pharmaceutical Sciences
Spyros P. Nikas: Center for Drug Discovery, Department of Pharmaceutical Sciences
Robert B. Laprairie: The Scripps Research Institute
Yiran Wu: iHuman Institute, ShanghaiTech University
Lu Qu: iHuman Institute, ShanghaiTech University
Mengchen Pu: iHuman Institute, ShanghaiTech University
Anisha Korde: Center for Drug Discovery, Department of Pharmaceutical Sciences
Shan Jiang: Center for Drug Discovery, Department of Pharmaceutical Sciences
Jo-Hao Ho: The Scripps Research Institute
Gye Won Han: Bridge Institute, University of Southern California
Kang Ding: iHuman Institute, 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
Laura M. Bohn: The Scripps Research Institute
Alexandros Makriyannis: Center for Drug Discovery, Department of Pharmaceutical Sciences
Raymond C. Stevens: iHuman Institute, ShanghaiTech University
Zhi-Jie Liu: iHuman Institute, ShanghaiTech University

Nature, 2017, vol. 547, issue 7664, 468-471

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.

Date: 2017
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DOI: 10.1038/nature23272

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