Skip to main content
. Author manuscript; available in PMC: 2017 Oct 26.
Published in final edited form as: Biochemistry. 2016 Nov 2;55(45):6327–6336. doi: 10.1021/acs.biochem.6b00932

Figure 1.

Figure 1

Domain structure of PKCα, PKCε and their mutants. Mutants (α/εC2, α/εC1, ε/αC2, ε/αC1, ε/αC1A, and ε/αC1B) were constructed by swapping the C1 and C2 domains of PKCα (αWT) and PKCε (εWT). C1A is the first diacylglycerol/phorbol ester binding domain; C1B is the second diacylglycerol/phorbol ester binding domain; C2 is the Ca++ and/or phospholipid binding domain; PS is the pseudosubstrate domain and C3 and C4 are kinase domain. All constructs have enhanced green fluorescent protein (EGFP) at the C-terminus.