Chemical shift assignments of the C-terminal domain of CaBP1 bound to the IQ-motif of voltage-gated Ca2+ channel (CaV1.2)

Abstract

The neuronal L-type voltage-gated Ca²⁺ channel (Ca_V1.2) interacts with Ca²⁺ binding protein 1 (CaBP1), that promotes Ca²⁺-induced channel activity. The binding of CaBP1 to the IQ-motif in Ca_V1.2 (residues 1644–1665) blocks the binding of calmodulin and prevents Ca²⁺-dependent inactivation of Ca_V1.2. This Ca²⁺-induced binding of CaBP1 to Ca_V1.2 is important for modulating neuronal synaptic plasticity, which may serve a role in learning and memory. Here we report NMR assignments of the C-terminal domain of CaBP1 (residues 99–167, called CaBP1C) that contains two Ca²⁺ bound at the third and fourth EF-hands (EF3 and EF4) and is bound to the Ca_V1.2 IQ-motif from Ca_V1.2 (BMRB accession no. 51518).