A multipronged approach for compiling a global map of allosteric regulation in the apoptotic caspases.

ABSTRACT: One of the most promising and as yet underutilized means of regulating protein function is exploitation of allosteric sites. All caspases catalyze the same overall reaction, but they perform different biological roles and are differentially regulated. It is our hypothesis that many allosteric sites exist on various caspases and that understanding both the distinct and overlapping mechanisms by which each caspase can be allosterically controlled should ultimately enable caspase-specific inhibition. Here we describe the ongoing work and methods for compiling a comprehensive map of apoptotic caspase allostery. Central to this approach are the use of (i) the embedded record of naturally evolved allosteric sites that are sensitive to zinc-mediated inhibition, phosphorylation, and other posttran

SUBMITTER: Dagbay K 

PROVIDER: S-EPMC4237280 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature