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Article

Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition.

Neuron - 10 Jan 2008

Gielen Marc, Le Goff Anne, Stroebel David, Johnson Jon W, Neyton Jacques, Paoletti Pierre

Abstract excerpt

Ionotropic glutamate receptor (iGluR) subunits contain a large N-terminal domain (NTD) that precedes the agonist-binding domain (ABD) and participates in subunit oligomerization. In NMDA receptors (NMDARs), the NTDs of NR2A and NR2B subunits also form binding sites for the endogenous inhibitor Zn(2+) ion. Although these allosteric sites have been characterized in detail, the molecular mechanisms by which the NTDs...

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Identifiers

PMID: 18184566
DOI: 10.1016/j.neuron.2007.11.021
PMCID: PMC2679256

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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