Cited by 181Neuroscience and Neuropharmacology ResearchAmino Acid Enzymes and MetabolismReceptor Mechanisms and Signaling

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Identification and Mechanism of Action of Two Histidine Residues Underlying High-Affinity Zn2+ Inhibition of the NMDA Receptor

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Choi, Yun-Beom, Lipton, Stuart A·1999·Neuron

DOI 10.1016/s0896-6273(00)80763-1

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Abstract

Zinc (Zn2+) inhibition of N-methyl-D-aspartate receptor (NMDAR) activity involves both voltage-independent and voltage-dependent components. Recombinant NR1/NR2A and NR1/NR2B receptors exhibit similar voltage-dependent block, but voltage-independent Zn2+ inhibition occurs with much higher affinity for NR1/NR2A than NR1/NR2B receptors (nanomolar versus micromolar IC50, respectively). Here, we show that two neighboring histidine residues on NR2A represent the critical determinant (termed the "short spacer") for high-affinity, voltage-independent Zn2+ inhibition using the Xenopus oocyte expression system and site-directed mutagenesis. Mutation of either one of these two histidine residues (H42 and H44) in the extracellular N-terminal domain of NR2A shifted the IC50 for high-affinity Zn2+ inhibition approximately 200-fold without affecting the EC50 of the coagonists NMDA and glycine. We suggest that the mechanism of high-affinity Zn2+ inhibition on the NMDAR involves enhancement of proton inhibition.

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Authors: Choi, Y.-B., & Lipton, S. A.
Affiliations: Brigham and Women's Hospital (US)
Corresponding author: Lipton, Stuart A
ORCID: Choi, Yun-Beom
Lipton, Stuart A
Venue: Neuron
Publisher: Elsevier BV
Published: 1999-05
Volume: 23
Issue: 1
Pages: 171-180
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/s0896-6273(00)80763-1
OpenAlex: W1970564284
Cited by: 180
References: 48
Citations by year: 2025: 2 · 2024: 1 · 2022: 4 · 2021: 2 · 2020: 4 · 2019: 3 · 2018: 7 · 2017: 4 · 2016: 8 · 2015: 5 · 2014: 10 · 2013: 4 · 2012: 12
FWCI: 3.71
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 5191 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Eye Institute (R01EY005477)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (P01HD029587)
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: zinc inhibition, NMDA receptor, NR2A subunit, histidine residues, voltage-dependent block, proton inhibition, site-directed mutagenesis
MeSH terms: Animals, Diethyl Pyrocarbonate, Female, Histidine, Mutation, Oocytes, Xenopus laevis, Zinc, Receptors, N-Methyl-D-Aspartate, Patch-Clamp Techniques, Protein Isoforms

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Identification and Mechanism of Action of Two Histidine Residues Underlying High-Affinity Zn2+ Inhibition of the NMDA Receptor

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