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Chemical shift assignments of a calmodulin intermediate with two Ca2+ bound in complex with the IQ-motif of voltage-gated Ca2+ channels (CaV1.2)

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Abstract

Calcium-dependent inactivation (CDI) of neuronal voltage-gated Ca2+ channels (CaV1.2) is important for synaptic plasticity, which is associated with learning and memory. The Ca2+-dependent binding of calmodulin (CaM) to CaV1.2 is essential for CDI. Here we report NMR assignments for a CaM mutant (D21A/D23A/D25A/E32Q/D57A/D59A/N61A/E68Q, called CaMEF12) that contains two Ca2+ bound at the third and fourth EF-hands (EF3 and EF4) and is bound to the IQ-motif (residues 1644–1665) from CaV1.2 (BMRB accession no. 27692).

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Acknowledgements

We thank Jeff Walton for technical support and help with NMR experiments. Work supported by NIH Grants (EY012347) to JBA and (AG055357) to JWH.

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Correspondence to James B. Ames.

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Salveson, I., Anderson, D.E., Hell, J.W. et al. Chemical shift assignments of a calmodulin intermediate with two Ca2+ bound in complex with the IQ-motif of voltage-gated Ca2+ channels (CaV1.2). Biomol NMR Assign 13, 233–237 (2019). https://doi.org/10.1007/s12104-019-09883-0

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