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Glycine receptors
A strychnine-insensitive glycine-binding site exists on the NMDA receptor. This site needs to be occupied by giycine to enable activation of the receptor [see Glutamate receptors (ionotropi:)].
The inhibitory glycine receptor is a pentamer of homologous 48 kDa and 58 kDa subunits which form an intrinsic Cl- channel. Four different isoforms of the a-subunit (al-&) and one variant of the fi-subunit (pl) have been identified by genomic and cDNA cloning. The a-subunit bears the l&and-binding site. All subunits have four transmembrane domains. Cl- flux is stimulated by glycine and antagonized by strychnine. Adult glycine receptor has a higher affinity for strychnine (pAz = 8.0) than the neonatal glycine receptor (pA2 = 7.0).
The inhibitory glycine receptor is a pentamer of homologous 48 kDa and 58 kDa subunits which form an intrinsic Cl- channel. Four different isoforms of the a-subunit (al-&) and one variant of the fi-subunit (pl) have been identified by genomic and cDNA cloning. The a-subunit bears the l&and-binding site. All subunits have four transmembrane domains. Cl- flux is stimulated by glycine and antagonized by strychnine. Adult glycine receptor has a higher affinity for strychnine (pAz = 8.0) than the neonatal glycine receptor (pA2 = 7.0).