ArticleNeuron2016
Molecular Basis for Subtype Specificity and High-Affinity Zinc Inhibition in the GluN1-GluN2A NMDA Receptor Amino-Terminal Domain.
Article in Neuron, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 79 citations in OpenAlex.
- Article
- Dynamic control of NMDA receptor CaProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Natural aminosterols inhibit NMDA receptors with low nanomolar potency.The FEBS journal · 2025Article
- Prospects and challenges in NMDAR signaling in spinal cord injury recovery and neural circuit remodeling.Regenerative therapy · 2025Review
- Evaluation of allosteric N-methyl-d-aspartate receptor modulation by GluN2A-selective antagonists using pharmacological equilibrium modeling.Molecular pharmacology · 2025Article
- Structural and functional mechanisms of anti-NMDAR autoimmune encephalitis.Nature structural & molecular biology · 2024Article
- Article
- Discovery of GluN2A subtype-selectiveActa pharmaceutica Sinica. B · 2024Review
- Structure and function of GluN1-3A NMDA receptor excitatory glycine receptor channel.Science advances · 2024Article
- N-Methyl-D-Aspartate (NMDA) Receptor Antagonists and their Pharmacological Implication: A Medicinal Chemistry-oriented Perspective Outline.Current medicinal chemistry · 2024Review
- Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023Review
- GluD receptors are functional ion channels.Biophysical journal · 2023Review
- Pharmacological Potential of 3-Benzazepines in NMDAR-Linked Pathophysiological Processes.Biomedicines · 2023Review
- Progresses in GluN2A-containing NMDA Receptors and their Selective Regulators.Cellular and molecular neurobiology · 2023Review
- Structural insights into assembly and function of GluN1-2C, GluN1-2A-2C, and GluN1-2D NMDARs.Molecular cell · 2022Article
- Development and characterization of functional antibodies targeting NMDA receptors.Nature communications · 2022Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- The diverse and complex modes of action of anti-NMDA receptor autoantibodies.Neuropharmacology · 2021Review
- GluN2A and GluN2B NMDA receptors use distinct allosteric routes.Nature communications · 2021Article
- Three-dimensional missense tolerance ratio analysis.Genome research · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Zinc is vastly present in the mammalian brain and controls functions of various cell surface receptors to regulate neurotransmission. A distinctive characteristic of N-methyl-D-aspartate (NMDA) receptors containing a GluN2A subunit is that their ion channel activity is allosterically inhibited by a nano-molar concentration of zinc that binds to an extracellular domain called an amino-terminal domain (ATD). Despite physiological importance, the molecular mechanism underlying the high-affinity zinc inhibition has been incomplete because of the lack of a GluN2A ATD structure. Here we show the first crystal structures of the heterodimeric GluN1-GluN2A ATD, which provide the complete map of the high-affinity zinc-binding site and reveal distinctive features from the ATD of the GluN1-GluN2B subtype. Perturbation of hydrogen bond networks at the hinge of the GluN2A bi-lobe structure affects both zinc inhibition and open probability, supporting the general model in which the bi-lobe motion in ATD regulates the channel activity in NMDA receptors.
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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.