Structural requirements for activation of the glycine receptor that modulates the N-methyl-D-aspartate operated ion channel

Lawrence D. Snell, Robert S. Morter, Kenneth M. Johnson

Research output: Contribution to journalArticle

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Abstract

It has recently been demonstrated that glycine can potentiate several measures of N-methyl-D-aspartate (NMDA)-induced channel opening, including radioligand binding to the PCP receptor. These data suggest that the NMDA/PCP receptor complex may be allosterically modulated by a binding site for glycine. We report here that several other monocarboxylic amino acids enhance NMDA-induced [3H]TCP binding and displace [3H]glycine binding with similar apparent affinities and stereoisomerism. The results are discussed with relation to the structural requirements for compounds to bind to this site.

Original languageEnglish (US)
Pages (from-to)105-110
Number of pages6
JournalEuropean Journal of Pharmacology
Volume156
Issue number1
DOIs
StatePublished - Oct 26 1988

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Keywords

  • (Binding)
  • Glycine
  • N-Methyl-D-aspartate (NMDA)
  • Phencyclidine
  • [H]1-[1-(2-Thienyl)cyclohexyl]piperidine ([H]TCP)

ASJC Scopus subject areas

  • Pharmacology

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