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

Hassaine, Ghérici and Deluz, Cédric and Grasso, Luigino and Wyss, Romain and Tol, Menno B. and Hovius, Ruud and Graff, Alexandra and Stahlberg, Henning and Tomizaki, Takashi and Desmyter, Aline and Moreau, Christophe and Li, Xiao-Dan and Poitevin, Frédéric and Vogel, Horst and Nury, Hugues. (2014) X-ray structure of the mouse serotonin 5-HT3 receptor. Nature, Vol. 512, H. 7514. pp. 276-281.

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Official URL: http://edoc.unibas.ch/dok/A6329110

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Stahlberg)
UniBasel Contributors:Stahlberg, Henning
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Macmillan
ISSN:0028-0836
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:06 Feb 2015 09:58
Deposited On:06 Feb 2015 09:58

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