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)
Article, Bibliographie
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.
| Item Type: | Article |
|---|---|
| Erschienen: | 1994 |
| Creators: | Kuryatov, A. ; Laube, Bodo ; Betz, H. ; Kuhse, J. |
| Type of entry: | Bibliographie |
| Title: | Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins. |
| Language: | English |
| Date: | 1994 |
| Journal or Publication Title: | Neuron |
| Volume of the journal: | 12 |
| Issue Number: | 6 |
| 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. |
| Divisions: | 10 Department of Biology 10 Department of Biology > Neurophysiology and Neurosensory Systems ?? fb10_zoologie ?? |
| Date Deposited: | 12 Apr 2011 11:21 |
| Last Modified: | 05 Mar 2019 06:48 |
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