Title : Three pairs of cysteine residues mediate both redox and zn2+ modulation of the nmda receptor.

Pub. Date : 2001 Jan 15

PMID : 11160420






3 Functional Relationships(s)
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1 Using site-directed mutagenesis, we identified three pairs of cysteine residues that underlie the various kinetic components of redox modulation of NMDA-evoked currents in Xenopus oocytes expressing NR1/NR2A receptors: (1) Cys 87 and Cys 320 in NR2A underlie the fast component, (2) Cys 79 and Cys 308 in NR1 underlie the intermediate component, and (3) Cys 744 and Cys 798 in NR1 underlie the persistent component. N-Methylaspartate glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis
2 Using site-directed mutagenesis, we identified three pairs of cysteine residues that underlie the various kinetic components of redox modulation of NMDA-evoked currents in Xenopus oocytes expressing NR1/NR2A receptors: (1) Cys 87 and Cys 320 in NR2A underlie the fast component, (2) Cys 79 and Cys 308 in NR1 underlie the intermediate component, and (3) Cys 744 and Cys 798 in NR1 underlie the persistent component. N-Methylaspartate glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis
3 Using site-directed mutagenesis, we identified three pairs of cysteine residues that underlie the various kinetic components of redox modulation of NMDA-evoked currents in Xenopus oocytes expressing NR1/NR2A receptors: (1) Cys 87 and Cys 320 in NR2A underlie the fast component, (2) Cys 79 and Cys 308 in NR1 underlie the intermediate component, and (3) Cys 744 and Cys 798 in NR1 underlie the persistent component. N-Methylaspartate glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis