Recent progress on the structure of Ser/Thr protein phosphatases

作     者：WANG BaiJing1,2, ZHANG Peng1 & WEI Qun1 1 Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing Key Laboratory, Beijing 100875, China 2 School of Life Science, Changchun Normal University, Changchun 130032, China 

作者机构：Department of Biochemistry and Molecular Biology Beijing Normal University Beijing Key Laboratory Beijing China School of Life Science Changchun Normal University Changchun China 

出 版 物：《Science China(Life Sciences)》 (中国科学（生命科学英文版）)

年 卷 期：2008年第51卷第6期

页      面：487-494页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 

基　　金：the National Basic Research Program of China (973) (Grant No. 2004CB719906) the National Natural Science Foundation of China (30470393) 

主　　题：Ser/Thr phosphatases subunit composition similarities and differences crystal structure 

摘      要：PP1, PP2A and PP2B, belonging to the PPP family of Ser/Thr protein phosphatases, participate in regulating many important physiological processes, such as cell cycle control, regulation of cell growth and division regulation, etc. The sequence homology between them is relatively high, and ter- tiary structure is conserved. Because of the complexity of the structure of PP2A and the diversity of its regulatory subunits, its structure is less well known than those of PP1 and PP2B. The PP2A holoen- zyme consists of a heterodimeric core enzyme, comprising a scaffolding subunit and a catalytic sub- unit, as well as a variable regulatory subunit. In this study, the subunit compositions, similarities and differences between the Ser/Thr protein phsphatases structures are summarized.