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.
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.
Gauss
C M
CM
Department of Chemistry, University of California at Irvine 92697, USA.
Sheppeck
J E
JE
Nairn
A C
AC
Chamberlin
R
R
D000595:Amino Acid Sequence; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019319:Okadaic Acid / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D004791:Enzyme Inhibitors; D019319:Okadaic Acid; D010749:Phosphoprotein Phosphatases