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

doi:10.1016/j.neuropharm.2006.12.002

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

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...

Topics

Animals
Binding, Competitive
Brain
Cell Line, Transformed
Cycloserine
Dose-Response Relationship, Drug
Excitatory Amino Acid Antagonists
Glycine
Humans
Kynurenic Acid
Models, Molecular
Mutation
Protein Binding
Rats
Receptors, N-Methyl-D-Aspartate
Transfection

Source

Open in PubMed

Identifiers

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

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics