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Article

Structural model of the N-methyl-D-aspartate receptor glycine site probed by site-directed chemical coupling.

The Journal of biological chemistry - 27 Jun 2003

Foucaud Bernard, Laube Bodo, Schemm Rudolf, Kreimeyer Annett, Goeldner Maurice, Betz Heinrich

Abstract excerpt

The N-methyl-d-aspartate (NMDA) receptor is a ligand-gated ion channel that requires both glutamate and glycine for efficient activation. Here, a strategy combining cysteine scanning mutagenesis and affinity labeling was used to investigate the glycine binding site located on the NR1 subunit. Based on homology modeling to the crystal structure of the glutamate binding site of the...

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Identifiers

PMID: 12697759
DOI: 10.1074/jbc.M300219200

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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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Structural model of the N-methyl-D-aspartate receptor glycine site probed by site-directed chemical coupling.PMID 12697759Read ↗

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