Structure and dynamics of the M3 muscarinic acetylcholine receptor

Andrew C. Kruse, Jianxin Hu, Albert C. Pan, Daniel H. Arlow, Daniel M. Rosenbaum, Erica Rosemond, Hillary F. Green, Tong Liu, Pil Seok Chae, Ron O. Dror, David E. Shaw, William I. Weis, Jürgen Wess () and Brian K. Kobilka ()
Additional contact information
Andrew C. Kruse: Stanford University School of Medicine, 279 Campus Drive
Jianxin Hu: Molecular Signaling Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases
Albert C. Pan: D. E. Shaw Research
Daniel H. Arlow: D. E. Shaw Research
Daniel M. Rosenbaum: University of Texas Southwestern Medical Center
Erica Rosemond: Molecular Signaling Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases
Hillary F. Green: D. E. Shaw Research
Tong Liu: Molecular Signaling Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases
Pil Seok Chae: Hanyang University, Ansan 426-791, Korea
Ron O. Dror: D. E. Shaw Research
David E. Shaw: D. E. Shaw Research
William I. Weis: Stanford University School of Medicine, 279 Campus Drive
Jürgen Wess: Molecular Signaling Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases
Brian K. Kobilka: Stanford University School of Medicine, 279 Campus Drive

Nature, 2012, vol. 482, issue 7386, 552-556

Abstract: The X-ray crystal structure of the M3 muscarinic acetylcholine receptor bound to the bronchodilator drug tiotropium is reported; comparison of this structure with that of the M2 muscarinic acetylcholine receptor reveals key differences that could potentially be exploited to develop subtype-selective drugs.

Date: 2012
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DOI: 10.1038/nature10867

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