A molecular modeling analysis of the binding interactions between the okadaic acid class of natural product inhibitors and the ser-thr phosphatases, PP1 and PP2A

Abstract We have proposed computer-generated models of the catalytic subunits of the serine-threonine protein phosphatases PP1 and PP2A complexed with their endogenous substrate phospho-DARPP-32, and several known naturally occurring inhibitors. This study is part of an overall effort to elucidate the signal transduction pathways in which PP1 and PP2A may play an important role.