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Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist

Author

Listed:
  • Kazuko Haga

    (Faculty of Science, Gakushuin University, Mejiro 1-5-1, Tokyo 171-8588, Japan)

  • Andrew C. Kruse

    (Stanford University School of Medicine, 279 Campus Drive)

  • Hidetsugu Asada

    (Kyoto University Faculty of Medicine, Konoe-cho, Yoshdida, Sakyo-Ku, Kyoto 606-8501, Japan
    Human Receptor Crystallography Project, ERATO, Japan Science and Technology Agency, Konoe-cho, Yoshida, Sakyo-Ku, Kyoto 606-8501, Japan)

  • Takami Yurugi-Kobayashi

    (Kyoto University Faculty of Medicine, Konoe-cho, Yoshdida, Sakyo-Ku, Kyoto 606-8501, Japan
    Human Receptor Crystallography Project, ERATO, Japan Science and Technology Agency, Konoe-cho, Yoshida, Sakyo-Ku, Kyoto 606-8501, Japan)

  • Mitsunori Shiroishi

    (Human Receptor Crystallography Project, ERATO, Japan Science and Technology Agency, Konoe-cho, Yoshida, Sakyo-Ku, Kyoto 606-8501, Japan
    Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan)

  • Cheng Zhang

    (Stanford University School of Medicine, 279 Campus Drive)

  • William I. Weis

    (Stanford University School of Medicine, 279 Campus Drive
    Stanford University School of Medicine, 299 Campus Drive)

  • Tetsuji Okada

    (Faculty of Science, Gakushuin University, Mejiro 1-5-1, Tokyo 171-8588, Japan)

  • Brian K. Kobilka

    (Stanford University School of Medicine, 279 Campus Drive)

  • Tatsuya Haga

    (Faculty of Science, Gakushuin University, Mejiro 1-5-1, Tokyo 171-8588, Japan)

  • Takuya Kobayashi

    (Kyoto University Faculty of Medicine, Konoe-cho, Yoshdida, Sakyo-Ku, Kyoto 606-8501, Japan
    Human Receptor Crystallography Project, ERATO, Japan Science and Technology Agency, Konoe-cho, Yoshida, Sakyo-Ku, Kyoto 606-8501, Japan
    Japan Science and Technology Agency, Core Research for Evolutional Science and Technology (CREST), Kyoto University Faculty of Medicine, Kyoto 606-8501, Japan)

Abstract

The X-ray crystal structure of the M2 muscarinic acetylcholine receptor, which is essential for the physiological control of cardiovascular function, is reported.

Suggested Citation

  • Kazuko Haga & Andrew C. Kruse & Hidetsugu Asada & Takami Yurugi-Kobayashi & Mitsunori Shiroishi & Cheng Zhang & William I. Weis & Tetsuji Okada & Brian K. Kobilka & Tatsuya Haga & Takuya Kobayashi, 2012. "Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist," Nature, Nature, vol. 482(7386), pages 547-551, February.
    • Handle: RePEc:nat:nature:v:482:y:2012:i:7386:d:10.1038_nature10753
    DOI: 10.1038/nature10753
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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. Wessel A. C. Burger & Vi Pham & Ziva Vuckovic & Alexander S. Powers & Jesse I. Mobbs & Yianni Laloudakis & Alisa Glukhova & Denise Wootten & Andrew B. Tobin & Patrick M. Sexton & Steven M. Paul & Chri, 2023. "Xanomeline displays concomitant orthosteric and allosteric binding modes at the M4 mAChR," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    3. Jun Xu & Qinggong Wang & Harald Hübner & Yunfei Hu & Xiaogang Niu & Haoqing Wang & Shoji Maeda & Asuka Inoue & Yuyong Tao & Peter Gmeiner & Yang Du & Changwen Jin & Brian K. Kobilka, 2023. "Structural and dynamic insights into supra-physiological activation and allosteric modulation of a muscarinic acetylcholine receptor," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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