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Mechanism of intracellular allosteric β2AR antagonist revealed by X-ray crystal structure

Author

Listed:
  • Xiangyu Liu

    (Beijing Advanced Innovation Center for Structural Biology, School of Medicine, Tsinghua University)

  • Seungkirl Ahn

    (Duke University Medical Center, Durham)

  • Alem W. Kahsai

    (Duke University Medical Center, Durham)

  • Kai-Cheng Meng

    (School of Pharmaceutical Engineering and Life Science, Changzhou University)

  • Naomi R. Latorraca

    (Stanford University
    Institute for Computational and Mathematical Engineering, Stanford University)

  • Biswaranjan Pani

    (Duke University Medical Center, Durham)

  • A. J. Venkatakrishnan

    (Stanford University
    Institute for Computational and Mathematical Engineering, Stanford University
    Stanford University School of Medicine)

  • Ali Masoudi

    (Duke University Medical Center, Durham)

  • William I. Weis

    (Stanford University School of Medicine)

  • Ron O. Dror

    (Stanford University
    Institute for Computational and Mathematical Engineering, Stanford University)

  • Xin Chen

    (School of Pharmaceutical Engineering and Life Science, Changzhou University)

  • Robert J. Lefkowitz

    (Duke University Medical Center, Durham
    Duke University Medical Center
    Howard Hughes Medical Institute, Duke University Medical Center)

  • Brian K. Kobilka

    (Beijing Advanced Innovation Center for Structural Biology, School of Medicine, Tsinghua University
    Stanford University School of Medicine)

Abstract

The authors report the crystal structure of the β2 adrenergic receptor in complex with compound 15, an allosteric modulator that binds to an alternative binding pocket.

Suggested Citation

  • Xiangyu Liu & Seungkirl Ahn & Alem W. Kahsai & Kai-Cheng Meng & Naomi R. Latorraca & Biswaranjan Pani & A. J. Venkatakrishnan & Ali Masoudi & William I. Weis & Ron O. Dror & Xin Chen & Robert J. Lefko, 2017. "Mechanism of intracellular allosteric β2AR antagonist revealed by X-ray crystal structure," Nature, Nature, vol. 548(7668), pages 480-484, August.
    • Handle: RePEc:nat:nature:v:548:y:2017:i:7668:d:10.1038_nature23652
    DOI: 10.1038/nature23652
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    Cited by:

    1. Xin Chen & Kexin Wang & Jianfang Chen & Chao Wu & Jun Mao & Yuanpeng Song & Yijing Liu & Zhenhua Shao & Xuemei Pu, 2024. "Integrative residue-intuitive machine learning and MD Approach to Unveil Allosteric Site and Mechanism for β2AR," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Janik B. Hedderich & Margherita Persechino & Katharina Becker & Franziska M. Heydenreich & Torben Gutermuth & Michel Bouvier & Moritz Bünemann & Peter Kolb, 2022. "The pocketome of G-protein-coupled receptors reveals previously untargeted allosteric sites," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    3. Jie Heng & Yunfei Hu & Guillermo Pérez-Hernández & Asuka Inoue & Jiawei Zhao & Xiuyan Ma & Xiaoou Sun & Kouki Kawakami & Tatsuya Ikuta & Jienv Ding & Yujie Yang & Lujia Zhang & Sijia Peng & Xiaogang N, 2023. "Function and dynamics of the intrinsically disordered carboxyl terminus of β2 adrenergic receptor," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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