Laube, Bodo ; Kuryatov, A. ; Kuhse, J. ; Betz, H. (1993)
Glycine-glutamate interactions at the NMDA receptor: role of cysteine residues.
In: FEBS letters, 335 (3)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
The NMDA subtype of ionotropic glutamate receptors occupation by both L-glutamate and the co-agonist glycine for efficient channel opening. To elucidate the role of disulfide bridges for the allosteric interaction of these agonists we mutated the cysteine residues in the ligand-binding NMDAR1 (NR1 or zeta) subunit of the rodent NMDA receptor and co-expressed the resulting mutants with the NR2B (epsilon 2) subunit in Xenopus oocytes. Most of the cysteine substitutions had no effect on agonist responses. However, replacement of cysteines 402 and 418 by alanine largely abolished the potentiation of glutamate currents by glycine. These cysteine residues in the putative extracellular domain of the NR1 subunit may form a disulfide bridge important for agonist interaction.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 1993 |
| Autor(en): | Laube, Bodo ; Kuryatov, A. ; Kuhse, J. ; Betz, H. |
| Art des Eintrags: | Bibliographie |
| Titel: | Glycine-glutamate interactions at the NMDA receptor: role of cysteine residues. |
| Sprache: | Englisch |
| Publikationsjahr: | 1993 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | FEBS letters |
| Jahrgang/Volume einer Zeitschrift: | 335 |
| (Heft-)Nummer: | 3 |
| Kurzbeschreibung (Abstract): | The NMDA subtype of ionotropic glutamate receptors occupation by both L-glutamate and the co-agonist glycine for efficient channel opening. To elucidate the role of disulfide bridges for the allosteric interaction of these agonists we mutated the cysteine residues in the ligand-binding NMDAR1 (NR1 or zeta) subunit of the rodent NMDA receptor and co-expressed the resulting mutants with the NR2B (epsilon 2) subunit in Xenopus oocytes. Most of the cysteine substitutions had no effect on agonist responses. However, replacement of cysteines 402 and 418 by alanine largely abolished the potentiation of glutamate currents by glycine. These cysteine residues in the putative extracellular domain of the NR1 subunit may form a disulfide bridge important for agonist interaction. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Neurophysiologie und neurosensorische Systeme ?? fb10_zoologie ?? |
| Hinterlegungsdatum: | 12 Apr 2011 11:26 |
| Letzte Änderung: | 05 Mär 2019 06:48 |
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