Characterization of CaMKIIα holoenzyme stability.

ABSTRACT: Ca²⁺ /calmodulin-dependent protein kinase II (CaMKII) is a Ser/Thr kinase necessary for long-term memory formation and other Ca²⁺ -dependent signaling cascades such as fertilization. Here, we investigated the stability of CaMKIIα using a combination of differential scanning calorimetry (DSC), X-ray crystallography, and mass photometry (MP). The kinase domain has a low thermal stability (apparent T_m = 36°C), which is slightly stabilized by ATP/MgCl₂ binding (apparent T_m = 40°C) and significantly stabilized by regulatory segment binding (apparent T_m = 60°C). We crystallized the kinase domain of CaMKII bound to p-coumaric acid in the active site. This structure reveals solvent-exposed hydrophobic residues in the substrate-bindi

SUBMITTER: Torres-Ocampo AP 

PROVIDER: S-EPMC7255518 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature