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X-ray structure of the mouse serotonin 5-HT3 receptor

Author

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  • Ghérici Hassaine

    (Laboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland
    Present address: Theranyx, 163 Avenue de Luminy, 13288 Marseille, France.)

  • Cédric Deluz

    (Laboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland)

  • Luigino Grasso

    (Laboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland)

  • Romain Wyss

    (Laboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland)

  • Menno B. Tol

    (Laboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland)

  • Ruud Hovius

    (Laboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland)

  • Alexandra Graff

    (Center for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, CH-4058 Basel, Switzerland)

  • Henning Stahlberg

    (Center for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, CH-4058 Basel, Switzerland)

  • Takashi Tomizaki

    (Swiss Light Source, Paul Scherrer Institute, CH-5234 Villigen, Switzerland)

  • Aline Desmyter

    (Architecture et Fonction des Macromolécules Biologiques, CNRS UMR 7257 and Université Aix-Marseille, F-13288 Marseille, France)

  • Christophe Moreau

    (Université Grenoble Alpes, IBS, F-38000 Grenoble, France
    CNRS, IBS, F-38000 Grenoble, France
    CEA, DSV, IBS, F-38000 Grenoble, France)

  • Xiao-Dan Li

    (Laboratory of Biomolecular Research, Paul Scherrer Institute, CH-5232 Villigen, Switzerland)

  • Frédéric Poitevin

    (Unité de Dynamique Structurale des Macromolécules, Institut Pasteur, CNRS UMR3528, F-75015 Paris, France)

  • Horst Vogel

    (Laboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland)

  • Hugues Nury

    (Laboratory of Physical Chemistry of Polymers and Membranes, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland
    Université Grenoble Alpes, IBS, F-38000 Grenoble, France
    CNRS, IBS, F-38000 Grenoble, France
    CEA, DSV, IBS, F-38000 Grenoble, France)

Abstract

Neurotransmitter-gated ion channels of the Cys-loop receptor family mediate fast neurotransmission throughout the nervous system. The molecular processes of neurotransmitter binding, subsequent opening of the ion channel and ion permeation remain poorly understood. Here we present the X-ray structure of a mammalian Cys-loop receptor, the mouse serotonin 5-HT3 receptor, at 3.5 Å resolution. The structure of the proteolysed receptor, made up of two fragments and comprising part of the intracellular domain, was determined in complex with stabilizing nanobodies. The extracellular domain reveals the detailed anatomy of the neurotransmitter binding site capped by a nanobody. The membrane domain delimits an aqueous pore with a 4.6 Å constriction. In the intracellular domain, a bundle of five intracellular helices creates a closed vestibule where lateral portals are obstructed by loops. This 5-HT3 receptor structure, revealing part of the intracellular domain, expands the structural basis for understanding the operating mechanism of mammalian Cys-loop receptors.

Suggested Citation

  • Ghérici Hassaine & Cédric Deluz & Luigino Grasso & Romain Wyss & Menno B. Tol & Ruud Hovius & Alexandra Graff & Henning Stahlberg & Takashi Tomizaki & Aline Desmyter & Christophe Moreau & Xiao-Dan Li , 2014. "X-ray structure of the mouse serotonin 5-HT3 receptor," Nature, Nature, vol. 512(7514), pages 276-281, August.
    • Handle: RePEc:nat:nature:v:512:y:2014:i:7514:d:10.1038_nature13552
    DOI: 10.1038/nature13552
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    Cited by:

    1. Eric Gibbs & Emily Klemm & David Seiferth & Arvind Kumar & Serban L. Ilca & Philip C. Biggin & Sudha Chakrapani, 2023. "Conformational transitions and allosteric modulation in a heteromeric glycine receptor," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. Marie S. Prevost & Nathalie Barilone & Gabrielle Dejean de la Bâtie & Stéphanie Pons & Gabriel Ayme & Patrick England & Marc Gielen & François Bontems & Gérard Pehau-Arnaudet & Uwe Maskos & Pierre , 2023. "An original potentiating mechanism revealed by the cryo-EM structures of the human α7 nicotinic receptor in complex with nanobodies," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    3. Nikhil Bharambe & Zhuowen Li & David Seiferth & Asha Manikkoth Balakrishna & Philip C. Biggin & Sandip Basak, 2024. "Cryo-EM structures of prokaryotic ligand-gated ion channel GLIC provide insights into gating in a lipid environment," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    4. Vasyl Bondarenko & Marta M. Wells & Qiang Chen & Tommy S. Tillman & Kevin Singewald & Matthew J. Lawless & Joel Caporoso & Nicole Brandon & Jonathan A. Coleman & Sunil Saxena & Erik Lindahl & Yan Xu &, 2022. "Structures of highly flexible intracellular domain of human α7 nicotinic acetylcholine receptor," Nature Communications, Nature, vol. 13(1), pages 1-9, December.

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