Journal article

ANTAGONISM OF LIGAND-GATED ION CHANNEL RECEPTORS - 2 DOMAINS OF THE GLYCINE RECEPTOR ALPHA-SUBUNIT FORM THE STRYCHNINE-BINDING SITE

RJ VANDENBERG, CR FRENCH, PH BARRY, J SHINE, PR SCHOFIELD

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | NATL ACAD PRESS | Published : 1992

Abstract

The inhibitory glycine receptor (GlyR) is a member of the ligand-gated ion channel receptor superfamily. Glycine activation of the receptor is antagonized by the convulsant alkaloid strychnine. Using in vitro mutagenesis and functional analysis of the cDNA encoding the alpha 1 subunit of the human GlyR, we have identified several amino acid residues that form the strychnine-binding site. These residues were identified by transient expression of mutated cDNAs in mammalian (293) cells and examination of resultant [3H]strychnine binding, glycine displacement of [3H]strychnine, and electrophysiological responses to the application of glycine and strychnine. This mutational analysis revealed that..

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