title: Recent progress on the structure of Ser/Thr protein phosphatases.
abstract: 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 tertiary 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 holoenzyme consists of a heterodimeric core enzyme, comprising a scaffolding subunit and a catalytic subunit, as well as a variable regulatory subunit. In this study, the subunit compositions, similarities and differences between the Ser/Thr protein phosphatases structures are summarized.
authors.affiliation: Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing Key Laboratory, Beijing 100875, China.
authors.forename: Baijing
authors.initials: B
authors.lastname: Wang
authors.forename: Peng
authors.initials: P
authors.lastname: Zhang
authors.forename: Qun
authors.initials: Q
authors.lastname: Wei
mesh_terms: D008958:Models, Molecular; D010749:Phosphoprotein Phosphatases / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D010749:Phosphoprotein Phosphatases