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Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation

Author

Listed:
  • Dean P. Staus

    (Duke University Medical Center)

  • Ryan T. Strachan

    (University of North Carolina)

  • Aashish Manglik

    (Stanford University School of Medicine)

  • Biswaranjan Pani

    (Duke University Medical Center)

  • Alem W. Kahsai

    (Duke University Medical Center)

  • Tae Hun Kim

    (University of Toronto, University of Toronto Mississauga)

  • Laura M. Wingler

    (Duke University Medical Center)

  • Seungkirl Ahn

    (Duke University Medical Center)

  • Arnab Chatterjee

    (Duke University Medical Center)

  • Ali Masoudi

    (Duke University Medical Center)

  • Andrew C. Kruse

    (Harvard Medical School)

  • Els Pardon

    (Structural Biology Brussels, Vrije Universiteit Brussel
    Structural Biology Research Center)

  • Jan Steyaert

    (Structural Biology Brussels, Vrije Universiteit Brussel
    Structural Biology Research Center)

  • William I. Weis

    (Stanford University School of Medicine
    Stanford University School of Medicine)

  • R. Scott Prosser

    (University of Toronto, University of Toronto Mississauga)

  • Brian K. Kobilka

    (Stanford University School of Medicine)

  • Tommaso Costa

    (Istituto Superiore di Sanità)

  • Robert J. Lefkowitz

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

Abstract

Stabilization of an active and inactive conformation of the β2-adrenergic receptor by allosteric nanobodies reveals differential ligand-dependent regulation of receptor states to control G-protein-coupled receptor activation.

Suggested Citation

  • Dean P. Staus & Ryan T. Strachan & Aashish Manglik & Biswaranjan Pani & Alem W. Kahsai & Tae Hun Kim & Laura M. Wingler & Seungkirl Ahn & Arnab Chatterjee & Ali Masoudi & Andrew C. Kruse & Els Pardon , 2016. "Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation," Nature, Nature, vol. 535(7612), pages 448-452, July.
    • Handle: RePEc:nat:nature:v:535:y:2016:i:7612:d:10.1038_nature18636
    DOI: 10.1038/nature18636
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    Cited by:

    1. Jia Duan & Peiyu Xu & Huibing Zhang & Xiaodong Luan & Jiaqi Yang & Xinheng He & Chunyou Mao & Dan-Dan Shen & Yujie Ji & Xi Cheng & Hualiang Jiang & Yi Jiang & Shuyang Zhang & Yan Zhang & H. Eric Xu, 2023. "Mechanism of hormone and allosteric agonist mediated activation of follicle stimulating hormone receptor," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Michael Schoof & Lan Wang & J. Zachery Cogan & Rosalie E. Lawrence & Morgane Boone & Jennifer Deborah Wuerth & Adam Frost & Peter Walter, 2021. "Viral evasion of the integrated stress response through antagonism of eIF2-P binding to eIF2B," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    3. Tobias Benkel & Mirjam Zimmermann & Julian Zeiner & Sergi Bravo & Nicole Merten & Victor Jun Yu Lim & Edda Sofie Fabienne Matthees & Julia Drube & Elke Miess-Tanneberg & Daniela Malan & Martyna Szpako, 2022. "How Carvedilol activates β2-adrenoceptors," Nature Communications, Nature, vol. 13(1), pages 1-20, December.
    4. Arum Wu & David Salom & John D. Hong & Aleksander Tworak & Kohei Watanabe & Els Pardon & Jan Steyaert & Hideki Kandori & Kota Katayama & Philip D. Kiser & Krzysztof Palczewski, 2023. "Structural basis for the allosteric modulation of rhodopsin by nanobody binding to its extracellular domain," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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