Journal
NATURE
Volume 512, Issue 7514, Pages 276-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature13552
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Funding
- Swiss National Science Foundation [31003A-133141]
- Ecole Polytechnique Federale de Lausanne
- European Community [211800]
- Human Frontier Science Program
- Agence Nationale de la Recherche (VenomPicoScreen project) [ANR-11-RPIB-022-04]
- Swiss National Science Foundation (SNF) [31003A_133141] Funding Source: Swiss National Science Foundation (SNF)
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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 angstrom 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 angstrom 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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