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Article

Allosteric signaling and dynamics of the clamshell-like NMDA receptor GluN1 N-terminal domain.

Nature structural & molecular biology - 1 Apr 2013

Zhu Shujia, Stroebel David, Yao C Andrea, Taly Antoine, Paoletti Pierre

Abstract excerpt

N-methyl-D-aspartate receptors (NMDARs), neuronal glutamate-gated ion channels, are obligatory heterotetramers composed of GluN1 and GluN2 subunits. Each subunit contains two extracellular clamshell-like domains with an agonist-binding domain and a distal N-terminal domain (NTD). The GluN2 NTDs form mobile regulatory domains. In contrast, the dynamics of GluN1 NTD and its contribution to NMDAR function remain...

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Identifiers

PMID: 23454977
DOI: 10.1038/nsmb.2522

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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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