ArticleThe Journal of biological chemistry2015
Kinetic contributions to gating by interactions unique to N-methyl-D-aspartate (NMDA) receptors.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- The positive allosteric modulator GNE-9278 increases gating, conductance, and CaNeuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2026Article
- Cryo-EM snapshots of NMDA receptor activation illuminate sequential rearrangements.Science advances · 2025Article
- Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- A structurally derived model of subunit-dependent NMDA receptor function.The Journal of physiology · 2018Article
- Structure, function, and allosteric modulation of NMDA receptors.The Journal of general physiology · 2018Review
- Kinetic models for activation and modulation of NMDA receptor subtypes.Current opinion in physiology · 2018Article
- How does binding of agonist ligands control intrinsic molecular dynamics in human NMDA receptors?PloS one · 2018Article
- The structure-energy landscape of NMDA receptor gating.Nature chemical biology · 2017Article
- Probing the Structural Dynamics of the NMDA Receptor Activation by Coarse-Grained Modeling.Biophysical journal · 2017Article
- Residues in the GluN1 C-terminal domain control kinetics and pharmacology of GluN1/GluN3A N-methyl-d-aspartate receptors.Neuropharmacology · 2017Article
- Gating Motions and Stationary Gating Properties of Ionotropic Glutamate Receptors: Computation Meets Electrophysiology.Accounts of chemical research · 2017Review
- The low binding affinity of D-serine at the ionotropic glutamate receptor GluD2 can be attributed to the hinge region.Scientific reports · 2017Article
- NMDA receptors: linking physiological output to biophysical operation.Nature reviews. Neuroscience · 2017Review
- NMDA Receptors in the Central Nervous System.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Differential effects of TM4 tryptophan mutations on inhibition of N-methyl-d-aspartate receptors by ethanol and toluene.Alcohol (Fayetteville, N.Y.) · 2016Article
- Structural Basis for Negative Allosteric Modulation of GluN2A-Containing NMDA Receptors.Neuron · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Among glutamate-gated channels, NMDA receptors produce currents that subside with unusually slow kinetics, and this feature is essential to the physiology of central excitatory synapses. Relative to the homologous AMPA and kainate receptors, NMDA receptors have additional intersubunit contacts in the ligand binding domain that occur at both conserved and non-conserved sites. We examined GluN1/GluN2A single-channel currents with kinetic analyses and modeling to probe these class-specific intersubunit interactions for their role in glutamate binding and receptor gating. We found that substitutions that eliminate such interactions at non-conserved sites reduced stationary gating, accelerated deactivation, and imparted sensitivity to aniracetam, an AMPA receptor-selective positive modulator. Abolishing unique contacts at conserved sites also reduced stationary gating and accelerated deactivation. These results show that contacts specific to NMDA receptors, which brace the heterodimer interface within the ligand binding domain, stabilize actively gating receptor conformations and result in longer bursts and slower deactivations. They support the view that the strength of the heterodimer interface modulates gating in both NMDA and non-NMDA receptors and that unique interactions at this interface are responsible in part for basic differences between the kinetics of NMDA and non-NMDA currents at glutamatergic synapses.
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