%0 Journal Article
%T Recent progress on the structure of Ser/Thr protein phosphatases<br>
%A BaiJing Wang
%A Peng Zhang
%A Qun Wei
%A <br>
%J 中国科学C辑(英文版)
%D 2008
%I Springer
%X 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.
%K Ser/Thr phosphatases
%K subunit composition
%K similarities and differences
%K crystal structure<br>
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=180CF3A72E750F3261A8A60EDC957784&aid=2EAB9F8A752DC0A5F89478C61ACB05C3&yid=67289AFF6305E306&vid=987EDA49D8A7A635&iid=B31275AF3241DB2D&sid=036D726259190A01&eid=3F419E61BD389CC8&journal_id=1674-7305&journal_name=ScienceChina.Lifesciences&referenced_num=0&reference_num=31