[HTML][HTML] Characterization of a Protein Kinase C-δ (PKC-δ) ATP Binding Mutant: AN INACTIVE ENZYME THAT COMPETITIVELY INHIBITS WILD TYPE PKC-δ …
W Li, JC Yu, DY Shin, JH Pierce - Journal of Biological Chemistry, 1995 - ASBMB
To investigate the function of protein kinase C (PKC)-δ, 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-δ cDNAs were generated either
with or without an influenza virus hemagglutinin epitope tag. After expression in 32D cells by
transfection, the PKC-δ ATP binding mutant (PKC-δK376R) was not able to phosphorylate
itself or the PKC-δ pseudosubstrate region-derived substrate, indicating that PKC-δK376R …
converting the invariant lysine in the catalytic domain (amino acid 376) to an arginine.
Expression vectors containing wild type and mutant PKC-δ cDNAs were generated either
with or without an influenza virus hemagglutinin epitope tag. After expression in 32D cells by
transfection, the PKC-δ ATP binding mutant (PKC-δK376R) was not able to phosphorylate
itself or the PKC-δ pseudosubstrate region-derived substrate, indicating that PKC-δK376R …
