Mapping of calmodulin-binding domain of Ca2+/calmodulin-dependent protein kinase II from rat brain.
Recent molecular cloning experiments have identified a 25 amino-acid region as the calmodulin-binding domain of the alpha-subunit of rat brain Ca2+/calmodulin-dependent multifunctional protein kinase II (CaM-K II). Synthetic peptides, derived from the deduced amino-acid sequence encompassing this region, were examined for their ability to bind calmodulin in a calcium dependent manner and to inhibit the Ca2+/calmodulin-dependent autophosphorylation of CaM-K II. Comparison of these structure-function relationships highlighted a region of 5 amino-acids, which was essential for calmodulin interaction and inhibition of kinase activity. This region demonstrated some homology with other calmodulin-binding peptides, and may represent a key site of interaction of the kinase with calmodulin. These analyses provide additional insight into the molecular mechanism underlying the Ca2+ regulation of CaM-K II.
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Related Subject Headings
- Rats
- Protein Kinases
- Protein Binding
- Phosphorylation
- Peptide Fragments
- Kinetics
- Calmodulin
- Calcium-Calmodulin-Dependent Protein Kinases
- Brain
- Biochemistry & Molecular Biology
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Rats
- Protein Kinases
- Protein Binding
- Phosphorylation
- Peptide Fragments
- Kinetics
- Calmodulin
- Calcium-Calmodulin-Dependent Protein Kinases
- Brain
- Biochemistry & Molecular Biology