Probing the determinants of diacylglycerol binding affinity in the C1B domain of protein kinase Cα.

ABSTRACT: C1 domains are independently folded modules that are responsible for targeting their parent proteins to lipid membranes containing diacylglycerol (DAG), a ubiquitous second messenger. The DAG binding affinities of C1 domains determine the threshold concentration of DAG required for the propagation of signaling response and the selectivity of this response among DAG receptors in the cell. The structural information currently available for C1 domains offers little insight into the molecular basis of their differential DAG binding affinities. In this work, we characterized the C1B domain of protein kinase Cα (C1Bα) and its diagnostic mutant, Y123W, using solution NMR methods and molecular dynamics simulations. The mutation did not perturb the C1Bα structure or the sub-nanosecond dynamics of t

SUBMITTER: Stewart MD 

PROVIDER: S-EPMC3489171 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature