Abstract
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 Ca2+-dependent desensitization of NMDAR channels. Mutations that disrupt Ca2+-dependent desensitization of NMDARs are linked to Alzheimer’s disease, depression, stroke, epilepsy, and schizophrenia. NMR chemical shift assignments are reported here for Ca2+-saturated CaM bound to the GluN2A C0 domain of NMDAR (BMRB no. 51821).
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Data availability
The assignments have been deposited to the BMRB under the accession code: 51821.
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Acknowledgements
We thank Derrick Kaseman and Ping Yu for help with NMR experiments performed at the UC Davis NMR Facility.
Funding
Work supported by NIH grants to J.B.A (R01 EY012347) and to the UC Davis NMR Facility (RR11973).
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A.B. performed all experiments, analyzed data and helped write the manuscript. J.B.A directed the overall project and wrote the manuscript.
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Bej, A., Ames, J.B. Chemical shift assignments of calmodulin bound to a cytosolic domain of GluN2A (residues 1004–1024) from the NMDA receptor. Biomol NMR Assign 17, 89–93 (2023). https://doi.org/10.1007/s12104-023-10125-7
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DOI: https://doi.org/10.1007/s12104-023-10125-7