ArticleMolecular pharmacology2012
Mapping the binding of GluN2B-selective N-methyl-D-aspartate receptor negative allosteric modulators.
Article in Molecular pharmacology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 46 citations in OpenAlex.
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- EAR-20 peptide, a novel NMDA receptor positive allosteric modulator.Frontiers in pharmacology · 2025Article
- Downstream Allosteric Modulation of NMDA Receptors by 3-Benzazepine Derivatives.Molecular neurobiology · 2023Article
- Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023Review
- Pharmacological Potential of 3-Benzazepines in NMDAR-Linked Pathophysiological Processes.Biomedicines · 2023Review
- Comparison of three novel radiotracers for GluN2B-containing NMDA receptors in non-human primates:Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2022Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Bidentatide, a Novel Plant Peptide Derived fromInternational journal of molecular sciences · 2021Article
- GRIN2D/GluN2D NMDA receptor: Unique features and its contribution to pediatric developmental and epileptic encephalopathy.European journal of paediatric neurology : EJPN : official journal of the European Paediatric Neurology Society · 2020Review
- Exploring the overlapping binding sites of ifenprodil and EVT-101 in GluN2B-containing NMDA receptors using novel chicken embryo forebrain cultures and molecular modeling.Pharmacology research & perspectives · 2019Article
- Synthesis and Preliminary Evaluations of a Triazole-Cored Antagonist as a PET Imaging Probe ([ACS chemical neuroscience · 2019Article
- Druggability Simulations and X-Ray Crystallography Reveal a Ligand-Binding Site in the GluA3 AMPA Receptor N-Terminal Domain.Structure (London, England : 1993) · 2019Article
- A common mechanism allows selective targeting of GluN2B subunit-containingCommunications biology · 2019Article
- Structure, function, and allosteric modulation of NMDA receptors.The Journal of general physiology · 2018Review
- BMS-986163, a Negative Allosteric Modulator of GluN2B with Potential Utility in Major Depressive Disorder.ACS medicinal chemistry letters · 2018Article
- NMDA Receptors in the Central Nervous System.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Mechanistic Insight into NMDA Receptor Dysregulation by Rare Variants in the GluN2A and GluN2B Agonist Binding Domains.American journal of human genetics · 2016Article
- A Novel Binding Mode Reveals Two Distinct Classes of NMDA Receptor GluN2B-selective Antagonists.Molecular pharmacology · 2016Article
- Emerging structural insights into the function of ionotropic glutamate receptors.Trends in biochemical sciences · 2015Review
- Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
We have used recent structural advances in our understanding of the N-methyl-d-aspartate (NMDA) receptor amino terminal domain to explore the binding mode of multiple diaryl GluN2B-selective negative allosteric modulators at the interface between the GluN1 and GluN2B amino-terminal domains. We found that interaction of the A ring within the binding pocket seems largely invariant for a variety of structurally distinct ligands. In addition, a range of structurally diverse linkers between the two aryl rings can be accommodated by the binding site, providing a potential opportunity to tune interactions with the ligand binding pocket via changes in hydrogen bond donors, acceptors, as well as stereochemistry. The most diversity in atomic interactions between protein and ligand occur in the B ring, with functional groups that contain electron donors and acceptors providing additional atomic contacts within the pocket. A cluster of residues distant to the binding site also control ligand potency, the degree of inhibition, and show ligand-induced increases in motion during molecular dynamics simulations. Mutations at some of these residues seem to distinguish between structurally distinct ligands and raise the possibility that GluN2B-selective ligands can be divided into multiple classes. These results should help facilitate the development of well tolerated GluN2B subunit-selective antagonists.
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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.