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

Neuron. 1992 Sep;9(3):491-6. doi: 10.1016/0896-6273(92)90186-h.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alanine / metabolism*
  • Amino Acid Sequence
  • Binding Sites
  • Binding, Competitive
  • Glycine / antagonists & inhibitors
  • Glycine / metabolism*
  • Humans
  • Ligands
  • Molecular Sequence Data
  • Mutation
  • Receptors, Glycine
  • Receptors, Neurotransmitter / chemistry
  • Receptors, Neurotransmitter / genetics
  • Receptors, Neurotransmitter / metabolism*
  • Strychnine / metabolism*
  • Taurine / metabolism*


  • Ligands
  • Receptors, Glycine
  • Receptors, Neurotransmitter
  • Taurine
  • Strychnine
  • Alanine
  • Glycine