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

97 Citations (Scopus)

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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Glycine Receptors
Phencyclidine Receptors
N-Methylaspartate
Ion Channels
Glycine
Stereoisomerism
N-Methyl-D-Aspartate Receptors
Binding Sites
Amino Acids

Keywords

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

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Pharmacology

Cite this

Structural requirements for activation of the glycine receptor that modulates the N-methyl-D-aspartate operated ion channel. / Snell, Lawrence D.; Morter, Robert S.; Johnson, Kenneth M.

In: European Journal of Pharmacology, Vol. 156, No. 1, 26.10.1988, p. 105-110.

Research output: Contribution to journalArticle

Snell, Lawrence D. ; Morter, Robert S. ; Johnson, Kenneth M. / Structural requirements for activation of the glycine receptor that modulates the N-methyl-D-aspartate operated ion channel. In: European Journal of Pharmacology. 1988 ; Vol. 156, No. 1. pp. 105-110.
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