Distinct agonist- and antagonist-binding sites on the glycine receptor
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.
|Authors||Vandenberg, R. J.;Handford, C. A.;Schofield, P. R. :|
|Published Date||1992-01-01 00:00:00|
|URL link to publisher's version||http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1326295|
|OpenAccess link to author's accepted manuscript version||https://publications.gimr.garvan.org.au/open-access/749|