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Journal articles
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.
https://hal-pasteur.archives-ouvertes.fr/pasteur-01721547
Contributor : Ana Cova Rodrigues Connect in order to contact the contributor
Submitted on : Friday, March 2, 2018 - 11:35:15 AM
Last modification on : Tuesday, October 19, 2021 - 10:28:03 PM
Contributor : Ana Cova Rodrigues Connect in order to contact the contributor
Submitted on : Friday, March 2, 2018 - 11:35:15 AM
Last modification on : Tuesday, October 19, 2021 - 10:28:03 PM
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