Characterization of a protein kinase C-delta (PKC-delta) ATP binding mutant. An inactive enzyme that competitively inhibits wild type PKC-delta enzymatic activity.

doi:10.1074/jbc.270.14.8311

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Article

Characterization of a protein kinase C-delta (PKC-delta) ATP binding mutant. An inactive enzyme that competitively inhibits wild type PKC-delta enzymatic activity.

The Journal of biological chemistry - 7 Apr 1995

Li W, Yu J C, Shin D Y, Pierce J H

Abstract excerpt

To investigate the function of protein kinase C (PKC)-delta, we mutated its ATP binding site by converting the invariant lysine in the catalytic domain (amino acid 376) to an arginine. Expression vectors containing wild type and mutant PKC-delta cDNAs were generated either with or without an influenza virus hemagglutinin epitope tag. After expression in 32D cells by transfection, the PKC-delta ATP binding mutant...

Topics

Adenosine Triphosphate
Animals
Base Sequence
Binding, Competitive
Cell Differentiation
Cell Line
Cell Membrane
Cloning, Molecular
DNA Primers
Isoenzymes
Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Monocytes

Mutation

Phosphorylation

Protein Binding

Protein Kinase C

Protein Kinase C-delta

Source

Open in PubMed

Identifiers

PMID: 7713939
DOI: 10.1074/jbc.270.14.8311

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7713939-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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