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

被引：49

作者：

Gauss, CM ^{[1
]}

Sheppeck, JE ^{[1
]}

Nairn, AC ^{[1
]}

Chamberlin, R ^{[1
]}

机构：

[1] ROCKEFELLER UNIV, NEW YORK, NY 10021 USA

来源：

BIOORGANIC & MEDICINAL CHEMISTRY | 1997年 / 5卷 / 09期

关键词：

D O I：

10.1016/S0968-0896(97)00145-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 1997 Published by Elsevier Science Ltd.

引用

页码：1751 / 1773

页数：23

共 24 条

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