Interactions of protein kinase C-α C1A and C1B domains with membranes: a combined computational and experimental study.

ABSTRACT: Protein kinase C-α (PKCα) has been studied widely as a paradigm for conventional PKCs, with two C1 domains (C1A and C1B) being important for the regulation and function of the kinase. However, it is challenging to explore these domains in membrane-bound environments with either simulations or experiments alone. In this work, we have combined modeling, simulations, and experiments to understand the molecular basis of the PKCα C1A and C1B domain interactions with membranes. Our atomistic simulations of the PKCα C1 domains reveal the dynamic interactions of the proteins with anionic lipids, as well as the conserved hydrogen bonds and the distinct nonpolar contacts formed with lipid activators. Corroborating evidence is obtained from additional simulations and experiments in terms of lipid bin

SUBMITTER: Li J 

PROVIDER: S-EPMC4140453 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature