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

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. Lefkowitz () and Brian K. Kobilka ()
Additional contact information
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
Biswaranjan Pani: Duke University Medical Center, Durham
A. J. Venkatakrishnan: Stanford University
Ali Masoudi: Duke University Medical Center, Durham
William I. Weis: Stanford University School of Medicine
Ron O. Dror: Stanford University
Xin Chen: School of Pharmaceutical Engineering and Life Science, Changzhou University
Robert J. Lefkowitz: Duke University Medical Center, Durham
Brian K. Kobilka: Beijing Advanced Innovation Center for Structural Biology, School of Medicine, Tsinghua University

Nature, 2017, vol. 548, issue 7668, 480-484

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.

Date: 2017
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DOI: 10.1038/nature23652

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