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

Kazuko Haga, Andrew C. Kruse, Hidetsugu Asada, Takami Yurugi-Kobayashi, Mitsunori Shiroishi, Cheng Zhang, William I. Weis, Tetsuji Okada, Brian K. Kobilka (), Tatsuya Haga () and Takuya Kobayashi ()
Additional contact information
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
Takami Yurugi-Kobayashi: Kyoto University Faculty of Medicine, Konoe-cho, Yoshdida, 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
Cheng Zhang: Stanford University School of Medicine, 279 Campus Drive
William I. Weis: Stanford University School of Medicine, 279 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

Nature, 2012, vol. 482, issue 7386, 547-551

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

Date: 2012
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DOI: 10.1038/nature10753

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