Article
Electrostatic and hydrophobic interactions differentially tune membrane binding kinetics of the C2 domain of protein kinase Cα.
The Journal of biological chemistry - 7 Jun 2013
Scott Angela M, Antal Corina E, Newton Alexandra C
Abstract excerpt
The cellular activation of conventional protein kinase C (PKC) isozymes is initiated by the binding of their C2 domains to membranes in response to elevations in intracellular Ca(2+). Following this C2 domain-mediated membrane recruitment, the C1 domain binds its membrane-embedded ligand diacylglycerol, resulting in activation of PKC. Here we explore the molecular mechanisms by which the C2 domain controls the...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
