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Chemical shift assignments of calmodulin bound to a cytosolic domain of GluN2A (residues 1004-1024) from the NMDA receptor

Biomol NMR Assign. 2023-04;

Aritra Bej, James B Ames

Products/Services Used	Details	Operation
Peptide Synthesis	… A peptide fragment of the GluN2A C0 domain of the NMDA receptor (residues 1004–1024) was purchased from GenScript. A 2.5-fold excess of the peptide was added to CaM and the …	Get A Quote

摘要

N-methyl-D-aspartate receptors (NMDARs) consist of glycine-binding GluN1 and glutamate-binding GluN2 subunits that form tetrameric ion channels. NMDARs in the neuronal post-synaptic membrane are important for controlling neuroplasticity and synaptic transmission in the brain. Calmodulin (CaM) binds to the cytosolic C0 domains of both GluN1 (residues 841-865) and GluN2 (residues 1004-1024) that may play a role in the Ca-dependent desensitization of NMDAR channels. Mutations that disrupt Ca-dependent desensitization of NMDARs are linked to Alzheimer's disease, depression, stroke, epilepsy, and schizophrenia. NMR chemical shift assignments are reported here for Ca-saturated CaM bound to the GluN2A C0 domain of NMD... More