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Article

Conformational transitions in the glycine-bound GluN1 NMDA receptor LBD via single-molecule FRET.

Biophysical journal - 7 Jul 2015

Cooper David R, Dolino Drew M, Jaurich Henriette, Shuang Bo, Ramaswamy Swarna, Nurik Caitlin E, Chen Jixin, Jayaraman Vasanthi, Landes Christy F

Abstract excerpt

The N-methyl-D-aspartate receptor (NMDAR) is a member of the glutamate receptor family of proteins and is responsible for excitatory transmission. Activation of the receptor is thought to be controlled by conformational changes in the ligand binding domain (LBD); however, glutamate receptor LBDs can occupy multiple conformations even in the activated form. This work probes equilibrium transitions among NMDAR LBD...

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Identifiers

PMID: 26153703
DOI: 10.1016/j.bpj.2015.05.025
PMCID: PMC4572502

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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