NMDA receptor subunits: function and pharmacology

PAOLETTI, P; NEYTON, J

doi:10.1016/j.coph.2006.08.011

Cited by 887Neuroscience and Neuropharmacology ResearchAmino Acid Enzymes and MetabolismReceptor Mechanisms and Signaling

NMDA receptor subunits: function and pharmacology

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PAOLETTI, P, NEYTON, J·2007·Current Opinion in Pharmacology

DOI 10.1016/j.coph.2006.08.011

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Abstract

N-methyl-D-aspartate receptors (NMDARs) are glutamate-gated ion channels widely expressed in the central nervous system that play key roles in excitatory synaptic transmission. Because of their involvement in numerous neurological disorders, NMDARs are also targets of therapeutic interest. NMDARs occur as multiple subtypes which differ in their subunit composition and in their biophysical and pharmacological properties. In particular, NMDARs contain a diversity of sites at which endogenous ligands or pharmacological agents can act to modulate receptor activity in a subunit-selective manner, and recent structural and functional data have started to reveal the molecular determinants for this subunit selectivity. These include the binding sites for glutamate, the ion-channel pore and the recently identified allosteric sites on the N-terminal domain. Other potential sites yet unexplored by medicinal chemistry programs are also considered, in particular at the interface between subunits. Given the growing body of evidence that diverse brain disorders implicate different NMDAR subtypes, such as NR2B in pain or NR3A in white matter injury, there is a growing interest in exploiting the pharmacological heterogeneity of NMDARs for the development of novel NMDAR subtype-selective compounds.

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NMDARs have two ligand-binding sites: GluN2 binds glutamate, while GluN1 and GluN3 bind glycine or D-serine, which is required for glutamate activation.
“The NMDAR has two ligand binding sites, with GluN2 binding to the primary agonist glutamate whereas GluN1 and GluN3 bind glycine or D-serine, in which binding is obligatory for activation by glutamate”
From Mechanisms of ketamine and its metabolites as antidepressants (2022) · cites this paper as Paoletti & Neyton, 2007
NMDA-receptors are glutamate-gated ion channels that play an important role in excitatory neurotransmission, plasticity, and excitotoxicity.
“NMDA-receptors are glutamate-gated ion channels, which play an important role in excitatory neurotransmission, plasticity, and excitotoxicity.11,12”
From Glutamate in Schizophrenia: A Focused Review and Meta-Analysis of 1H-MRS Studies (2013) · cites this paper as [12]

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Authors: PAOLETTI, P., & NEYTON, J.
Affiliations: Centre National de la Recherche Scientifique (FR)
Corresponding author: PAOLETTI, P
ORCID: PAOLETTI, P
Venue: Current Opinion in Pharmacology
Publisher: Elsevier BV
Published: 2007-02
Volume: 7
Issue: 1
Pages: 39-47
ISSN: 1471-4892 (ISSN-L)
DOI: 10.1016/j.coph.2006.08.011
OpenAlex: W2012641732
Cited by: 887
References: 63
Citations by year: 2026: 19 · 2025: 20 · 2024: 27 · 2023: 32 · 2022: 27 · 2021: 36 · 2020: 40 · 2019: 38 · 2018: 52 · 2017: 46 · 2016: 48 · 2015: 45 · 2014: 58 · 2013: 72 · 2012: 72
FWCI: 15.18
Type: journal article
Language: en
Open access: green
hal.science
Licence: other-oa
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Current Opinion in Pharmacology (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion, other-oa)
Funders: Agence Nationale de la Recherche
Institut National de la Santé et de la Recherche Médicale
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords: NMDA receptor, NMDA receptor subunits, glutamate binding site, ion channel pore, allosteric site, N-terminal domain, NR2B, subtype-selective ligands, excitatory synaptic transmission, neurological disorders, drug development
MeSH terms: Animals, Humans, Ligands, Myelin Sheath, Schizophrenia, Receptors, N-Methyl-D-Aspartate, Protein Structure, Tertiary, Protein Subunits

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NMDA receptor subunits: function and pharmacology

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