Protein tyrosine phosphatases: mechanisms of catalysis and regulation

被引：318

作者：

Denu, JM

Dixon, JE

机构：

[1] Oregon Hlth Sci Univ, Dept Biochem & Mol Biol L224, Portland, OR 97201 USA

[2] Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 48109 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 1998年 / 2卷 / 05期

关键词：

D O I：

10.1016/S1367-5931(98)80095-1

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：

Recent structural information suggests that the HC(X)(5)R active-site motif defines three distinct evolutionary families of phosphatases that employ a common catalytic mechanism. In two instances, regulation of phosphatase activity employs autoinhibitory mechanisms involving either intermolecular or intramolecular interactions, whereby inhibition is mediated by sterically blocking the active-site cleft.

引用

页码：633 / 641

页数：9

共 58 条

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