Binary-FRET reveals transient excited-state structure associated with activity-dependent CaMKII - NR2B binding and adaptation.

ABSTRACT: Synaptic functions are mediated and modulated by a coordinated choreography of protein conformational changes and interactions in response to intracellular calcium dynamics. Time-lapse Förster resonance energy transfer can be used to study the dynamics of both conformational changes and protein-protein interactions simultaneously under physiological conditions if two resonance energy transfer reactions can be multiplexed. Binary-FRET is a technique developed to independently monitor the dynamics of calcium-calmodulin dependent protein kinase-II catalytic-domain pair separation in the holoenzyme, and its role in establishing activity-dependent holoenzyme affinity for the NR2B binding fragment of the N-methyl-D-aspartate receptor. Here we show that a transient excited-state intermediate exis

SUBMITTER: Nguyen TA 

PROVIDER: S-EPMC9596428 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature