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Article

Mutational analysis of secondary structure in the autoinhibitory and autophosphorylation domains of calmodulin kinase II.

The Journal of biological chemistry - 12 Aug 1994

Mukherji S, Brickey D A, Soderling T R

Abstract excerpt

A previous study has suggested that the autoinhibitory domain of Ca2+/calmodulin-dependent protein kinase II (CaM-kinase II) may contain an alpha-helical structure, which is important for the proper orientation of inhibitory residues to interact with the catalytic domain (Smith, M. K., Colbran, R. J., Brickey, D. A., and Soderling, T.R. (1992) J. Biol. Chem. 267, 1761-1768). The present study was designed to test...

Topics

Amino Acid Sequence
Animals
Calcium
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Calcium-Calmodulin-Dependent Protein Kinases
Cells, Cultured
DNA Mutational Analysis
Enzyme Activation
Molecular Sequence Data
Moths

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Phosphorylation

Protein Structure, Secondary

Source

Identifiers

PMID: 8051174

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8051174-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Mutational analysis of secondary structure in the autoinhibitory and autophosphorylation domains of calmodulin kinase II.PMID 8051174Read ↗

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