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Distinct agonist- and antagonist-binding sites on the glycine receptor

Abstract

The distinction between receptor-binding sites for agonists and antagonists underpins the pharmacological differences between these two classes of ligands. In the glycine receptor, antagonist (strychnine) binding requires an interaction with residues Lys-200 and Tyr-202. We now demonstrate that the agonist-binding site of this receptor is located at the residue Thr-204. The agonist-binding site interaction is thus likely to be mediated by hydrogen bonding and not by ionic interactions. Our results demonstrate that, in contrast to other studies of ligand-gated ion channel receptors, agonist- and antagonist-binding sites are composed of distinct amino acid residues.

Type Journal
ISBN 0896-6273 (Print)
Authors Vandenberg, R. J.;Handford, C. A.;Schofield, P. R. :
Publisher Name NEURON
Published Date 1992-01-01 00:00:00
Published Volume 9
Published Issue 3
Published Pages 491-6
URL http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1326295
Status Published In-print