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

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Hassaine Ghérici, Deluz Cédric, Grasso Luigino, Wyss Romain, Tol Menno B, Hovius Ruud, Graff Alexandra, Stahlberg Henning, Tomizaki Takashi, Desmyter Aline, Moreau Christophe, Li Xiao-Dan, Poitevin Frédéric, Vogel Horst, Nury Hugues,
Project Electron Microscopy of Membrane Proteins
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Original article (peer-reviewed)

Journal Nature
Volume (Issue) 512(7514)
Page(s) 276 - 81
Title of proceedings Nature
DOI 10.1038/nature13552

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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