ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006
Characterization of a soluble ligand binding domain of the NMDA receptor regulatory subunit NR3A.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 110 citations in OpenAlex.
- Chronic Alcohol Exposure Alters Expression of GluN3A-NMDA Receptors in Adult VTA DA Neurons.bioRxiv : the preprint server for biology · 2026Article
- Structural and mechanistic insights into gating and allosteric modulation of GluN1-GluN3A NMDA receptors.Nature structural & molecular biology · 2026Article
- Non-classical NMDAR subunit GluN3A in a specialized hippocampal region regulates stress-coping strategies in male mice.Communications biology · 2026Article
- Discovery of selective GluN1/GluN3A NMDA receptor inhibitors using integrated AI and physics-based approaches.Acta pharmacologica Sinica · 2026Article
- Discovery of novel GluN1/GluN3A NMDA receptor inhibitors using a deep learning-based method.Acta pharmacologica Sinica · 2025Article
- Discrete interneuron subsets participate in GluN1/GluN3A excitatory glycine receptor (eGlyR)-mediated regulation of hippocampal network activity throughout development and evolution.Research square · 2025Article
- Discrete interneuron subsets participate in GluN1/GluN3A excitatory glycine receptor (eGlyR)-mediated regulation of hippocampal network activity throughout development and evolution.bioRxiv : the preprint server for biology · 2025Article
- Excitatory glycine receptors control ventral hippocampus synaptic plasticity and anxiety-related behaviors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Research Progress on NMDA Receptor Enhancement Drugs for the Treatment of Depressive Disorder.CNS drugs · 2024Review
- GluN3A and Excitatory Glycine Receptors in the Adult Hippocampus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- Structure and function of GluN1-3A NMDA receptor excitatory glycine receptor channel.Science advances · 2024Article
- D-Cycloserine enhances the bidirectional range of NMDAR-dependent hippocampal synaptic plasticity.Translational psychiatry · 2024Article
- Allosteric modulation of GluN1/GluN3 NMDA receptors by GluN1-selective competitive antagonists.The Journal of general physiology · 2023Article
- Article
- Derivatives of (Journal of medicinal chemistry · 2022Article
- Identification of a Subtype-Selective Allosteric Inhibitor of GluN1/GluN3 NMDA Receptors.Frontiers in pharmacology · 2022Article
- The roles of GluN3-containing N-methyl-D-aspartate receptor in central nerve system.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2021Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Allosteric coupling of sub-millisecond clamshell motions in ionotropic glutamate receptor ligand-binding domains.Communications biology · 2021Article
- The Extracellular Domains of GluN Subunits Play an Essential Role in Processing NMDA Receptors in the ER.Frontiers in neuroscience · 2021Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
Abstract
NR3A is expressed widely in the developing CNS of mammals. Coassembly of NR3A with NR1 and NR2 modifies NMDA receptor-mediated responses, reducing calcium permeability and single-channel conductance. The ligand binding properties of NR3A are unknown but shape the role NR3A plays when incorporated into NMDA receptors. Here, a soluble NR3A ligand binding domain (NR3A S1S2) was constructed based on amino acid sequence alignments with other glutamate receptor ion channels and is expressed in Escherichia coli. After purification by affinity, gel filtration, and ion exchange chromatography, NR3A S1S2 behaves as a monomer even at a concentration of 20 mg/ml, as determined by size-exclusion chromatography and dynamic light scattering. NR3A S1S2 has very high affinity for glycine with an apparent dissociation constant (Kd) of 40 nm, 650-fold less than the Kd for NR1. Glutamate, which binds to NR2 subunits, also binds to NR3A, but with very low affinity (Kd = 9.6 mm); in contrast, binding of glutamate to NR1 was not detectable even at a 300 mm concentration. The antagonist binding profiles of NR3A and NR1 also show striking differences. 6-cyano-2,3-dihydroxy-7-nitro-quinoxaline (CNQX), and its analog CGP78608, bind to NR3A S1S2 with low micromolar affinity, whereas for NR1, the affinity of CGP78608 increases 1000-fold compared with CNQX. Other high-affinity NR1 antagonists also show very weak binding to NR3A. Proteolysis protection experiments reveal that CNQX and CGP78608 bind to and stabilize domain 1 of NR3A S1S2 but increase proteolysis of domain 2, indicating that they produce conformational changes distinct from those induced by glycine and D-serine.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.