Kuryatov, A. ; Laube, Bodo ; Betz, H. ; Kuhse, J. (1994)
Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins.
In: Neuron, 12 (6)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
Activation of the NMDA subtype of ionotropic glutamate receptors requires binding of both L-glutamate and the coagonist glycine. Site-directed mutagenesis of the NMDAR1 (NR1) subunit revealed that aromatic residues at positions 390, 392, and 466 are crucial determinants of glycine binding. Glutamate efficacy was little affected by mutations at these positions; however, inhibition of channel gating by the glycine antagonist 7-chlorokynurenic acid was drastically reduced. In addition, glutamine (Q387), valine (V666), and serine (S669) substitutions were found to reduce glycine efficacy. Since the mutated residues correspond to positions forming the binding site of homologous bacterial amino acid-binding proteins, a common amino acid-binding fold appears to be conserved from prokaryotic periplasmic proteins to glutamate receptors in the mammalian brain.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 1994 |
| Autor(en): | Kuryatov, A. ; Laube, Bodo ; Betz, H. ; Kuhse, J. |
| Art des Eintrags: | Bibliographie |
| Titel: | Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins. |
| Sprache: | Englisch |
| Publikationsjahr: | 1994 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Neuron |
| Jahrgang/Volume einer Zeitschrift: | 12 |
| (Heft-)Nummer: | 6 |
| Kurzbeschreibung (Abstract): | Activation of the NMDA subtype of ionotropic glutamate receptors requires binding of both L-glutamate and the coagonist glycine. Site-directed mutagenesis of the NMDAR1 (NR1) subunit revealed that aromatic residues at positions 390, 392, and 466 are crucial determinants of glycine binding. Glutamate efficacy was little affected by mutations at these positions; however, inhibition of channel gating by the glycine antagonist 7-chlorokynurenic acid was drastically reduced. In addition, glutamine (Q387), valine (V666), and serine (S669) substitutions were found to reduce glycine efficacy. Since the mutated residues correspond to positions forming the binding site of homologous bacterial amino acid-binding proteins, a common amino acid-binding fold appears to be conserved from prokaryotic periplasmic proteins to glutamate receptors in the mammalian brain. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Neurophysiologie und neurosensorische Systeme ?? fb10_zoologie ?? |
| Hinterlegungsdatum: | 12 Apr 2011 11:21 |
| Letzte Änderung: | 05 Mär 2019 06:48 |
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