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Article

Characterisation of the human NMDA receptor subunit NR3A glycine binding site.

Neuropharmacology - 1 Mar 2007

Nilsson A, Duan J, Mo-Boquist L-L, Benedikz E, Sundström E

Abstract excerpt

In this study, we characterise the binding site of the human N-methyl-d-aspartate (NMDA) receptor subunit NR3A. Saturation radioligand binding of the NMDA receptor agonists [(3)H]-glycine and [(3)H]-glutamate showed that only glycine binds to human NR3A (hNR3A) with high affinity (K(d)=535nM (277-793nM)). Eight amino acids, which correspond to amino acids that are critical for ligand binding to other NMDA...

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Identifiers

PMID: 17320117
DOI: 10.1016/j.neuropharm.2006.12.002

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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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