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. Author manuscript; available in PMC: 2010 Jul 8.
Published in final edited form as: Physiol Rev. 2008 Oct;88(4):1341–1378. doi: 10.1152/physrev.00034.2007

FIG. 5.

FIG. 5

Alignment of kinase domain activation loops. A: Mg positioning loop (in green), activation loop phosphorylation site, invariant tyrosines that are phosphorylated in certain PKCs, and the unique structural features of PKCδ that recently have been considered a mechanism to render this isoform catalytically competent without activation loop phosphorylation are depicted. B: sequence alignment for the A-helix in PKCδ and protein kinase A (PKA) (see text). C: activation loop phosphorylation mechanisms and functions.