Ethanol Modulation is Quantitatively Determined by the Transmembrane Domain of Human α 1 Glycine Receptors - Institut Pasteur Access content directly
Journal Articles Alcoholism: Clinical and Experimental Research Year : 2015

Ethanol Modulation is Quantitatively Determined by the Transmembrane Domain of Human α 1 Glycine Receptors

Abstract

Mutagenesis and labeling studies have identified amino acids from the human α1 glycine receptor (GlyR) extracellular, transmembrane (TM), and intracellular domains in mediating ethanol (EtOH) potentiation. However, limited high-resolution structural data for physiologically relevant receptors in this Cys-loop receptor superfamily have made pinpointing the critical amino acids difficult. Homologous ion channels from lower organisms provide conserved models for structural and functional properties of Cys-loop receptors. We previously demonstrated that a single amino acid variant of the Gloeobacter violaceus ligand-gated ion channel (GLIC) produced EtOH and anesthetic sensitivity similar to that of GlyRs and provided crystallographic evidence for EtOH binding to GLIC.

Domains

Neuroscience

Dates and versions

pasteur-01721547 , version 1 (02-03-2018)

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Cite

Suzzane Horani, Evan P. Stater, Pierre-Jean Corringer, James Trudell, R. Adron Harris, et al.. Ethanol Modulation is Quantitatively Determined by the Transmembrane Domain of Human α 1 Glycine Receptors. Alcoholism: Clinical and Experimental Research, 2015, 39 (6), pp.962 - 968. ⟨10.1111/acer.12735⟩. ⟨pasteur-01721547⟩
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