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

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.
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Nature, Nature Publishing Group, 2014, 512, pp.276-81. 〈10.1038/nature13552〉
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http://hal.univ-grenoble-alpes.fr/hal-01102530
Contributeur : Frank Thomas <>
Soumis le : mardi 13 janvier 2015 - 09:28:35
Dernière modification le : lundi 10 septembre 2018 - 10:29:32

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Ghérici Hassaine, Cédric Deluz, Luigino Grasso, Romain Wyss, Menno B Tol, et al.. X-ray structure of the mouse serotonin 5-HT3 receptor. Nature, Nature Publishing Group, 2014, 512, pp.276-81. 〈10.1038/nature13552〉. 〈hal-01102530〉

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