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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.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-01721547
Contributor : Ana Cova Rodrigues <>
Submitted on : Friday, March 2, 2018 - 11:35:15 AM
Last modification on : Monday, January 13, 2020 - 5:08:17 PM

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Suzzane Horani, Evan 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, Wiley, 2015, 39 (6), pp.962 - 968. ⟨10.1111/acer.12735⟩. ⟨pasteur-01721547⟩

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