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

ABSTRACT: 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 conformations by monitoring the distance across the glycine-bound LBD cleft using single-molecule Förster resonance energy transfer (smFRET). Recent improvements in photoprotection solutions allowed us to monitor transitions among the multiple conformations. Also, we applied a recently developed model-free algorithm called "step transition and state identification" to identify the

SUBMITTER: Cooper DR 

PROVIDER: S-EPMC4572502 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature