Structural basis and functional analysis of NMDA receptor regulation by calmodulin.

ABSTRACT: The synaptic plasticity mechanisms that are thought to underlie learning and memory require Ca²⁺ influx mediated by N-methyl-D-aspartate receptors composed of glycine-binding GluN1 and glutamate-binding GluN2 subunits. Calmodulin (CaM) binding to the cytosolic regions in both GluN1 (residues 841-865, called GluN1-C0) and GluN2A (residues 1004-1023, called GluN2A-C0) may be important for Ca²⁺-dependent channel desensitization (CDD). Here, we report NMR, ITC and electrophysiological experiments to probe the structure and functional role of Ca²⁺-bound CaM (Ca²⁺-CaM) binding to both GluN1 and GluN2A subunits. Our ITC studies show that the GluN1-C0 peptide binds to both the N-lobe and C-lobe of Ca²⁺-CaM, whereas the GluN2A-C0 peptide binds

SUBMITTER: Bej A 

PROVIDER: S-EPMC12870862 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature