ArticleBiophysical journal2000
NMDA channel gating is influenced by a tryptophan residue in the M2 domain but calcium permeation is not altered.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Article
- Magnetic field effects in biology from the perspective of the radical pair mechanism.Journal of the Royal Society, Interface · 2022Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- De novo GRIN variants in NMDA receptor M2 channel pore-forming loop are associated with neurological diseases.Human mutation · 2019Article
- Article
- A novel alcohol-sensitive position in the N-methyl-D-aspartate receptor GluN2A subunit M3 domain regulates agonist affinity and ion channel gating.Molecular pharmacology · 2013Article
- Common binding site for externally and internally applied AMPA receptor channel blockers.Journal of molecular neuroscience : MN · 2009Article
- NR2 subunit-dependence of NMDA receptor channel block by external Mg2+.The Journal of physiology · 2005Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-Methyl-D-aspartate (NMDA) receptors are susceptible to open-channel block by dizolcipine (MK-801), ketamine and Mg(2+) and are permeable to Ca(2+). It is thought that a tryptophan residue in the second membrane-associated domain (M2) may form part of the binding site for open-channel blockers and contribute to Ca(2+) permeability. We tested this hypothesis using recombinant wild-type and mutant NMDA receptors expressed in HEK-293 cells. The tryptophan was mutated to a leucine (W-5L) in both the NMDAR1 and NMDAR2A subunits. MK-801 and ketamine progressively inhibited currents evoked by glutamate, and the rate of inhibition was increased by the W-5L mutation. An increase in open channel probability accounted for the acceleration. Fluctuation analysis of the glutamate-evoked current revealed that the NMDAR1 W-5L mutation increased channel mean open time, providing further evidence for an alteration in gating. However, the equilibrium affinities of Mg(2+) and ketamine were largely unaffected by the W-5L mutation, and Ca(2+) permeability was not decreased. Therefore, the M2 tryptophan residue of the NMDA channel is not involved in Ca(2+) permeation or the binding of open-channel blockers, but plays an important role in channel gating.
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