A MOLECULAR MODELING ANALYSIS OF THE BINDING INTERACTIONS BETWEEN THEOKADAIC ACID CLASS OF NATURAL PRODUCT INHIBITORS AND THE SER-THR PHOSPHATASES, PP1 AND PP2A
Cm. Gauss et al., A MOLECULAR MODELING ANALYSIS OF THE BINDING INTERACTIONS BETWEEN THEOKADAIC ACID CLASS OF NATURAL PRODUCT INHIBITORS AND THE SER-THR PHOSPHATASES, PP1 AND PP2A, Bioorganic & medicinal chemistry, 5(9), 1997, pp. 1751-1773
We have proposed computer-generated models of the catalytic subunits o
f the serine-threonine protein phosphatases PP1 and PP2A complexed wit
h their endogenous substrate phospho-DARPP-32, and several known natur
ally occurring inhibitors. This study is part of an overall effort to
elucidate the signal transduction pathways in which PP1 and PP2A may p
lay an important role. (C) 1997 Published by Elsevier Science Ltd.