Skip to main content
eScholarship
Open Access Publications from the University of California

UC Davis

UC Davis Previously Published Works bannerUC Davis

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 (CaV1.2) interacts with Ca2+ binding protein 1 (CaBP1), that promotes Ca2+-induced channel activity. The binding of CaBP1 to the IQ-motif in CaV1.2 (residues 1644-1665) blocks the binding of calmodulin and prevents Ca2+-dependent inactivation of CaV1.2. This Ca2+-induced binding of CaBP1 to CaV1.2 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 CaV1.2 IQ-motif from CaV1.2 (BMRB accession no. 51518).

Many UC-authored scholarly publications are freely available on this site because of the UC's open access policies. Let us know how this access is important for you.

Main Content
For improved accessibility of PDF content, download the file to your device.
Current View