Structural requirements for activation of the glycine receptor that modulates the N-methyl-D-aspartate operated ion channel.
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.
Snell
L D
LD
University of Texas Medical Branch, Galveston 77550.
Morter
R S
RS
Johnson
K M
KM
D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D001224:Aspartic Acid / Q000031:analogs & derivatives* / Q000494:pharmacology; D002540:Cerebral Cortex / Q000378:metabolism; D005998:Glycine / Q000502:physiology*; D007473:Ion Channels / Q000187:drug effects* / Q000502:physiology; D016202:N-Methylaspartate; D010622:Phencyclidine / Q000031:analogs & derivatives / Q000378:metabolism; D051381:Rats; D018009:Receptors, Glycine; D017981:Receptors, Neurotransmitter / Q000502:physiology*
D000596:Amino Acids; D007473:Ion Channels; D018009:Receptors, Glycine; D017981:Receptors, Neurotransmitter; D001224:Aspartic Acid; D016202:N-Methylaspartate; C012058:tenocyclidine; D010622:Phencyclidine; D005998:Glycine