Science in China Series C: Life Sciences

, Volume 51, Issue 6, pp 487–494

Recent progress on the structure of Ser/Thr protein phosphatases

Article

DOI: 10.1007/s11427-008-0068-y

Cite this article as:
Wang, B., Zhang, P. & Wei, Q. SCI CHINA SER C (2008) 51: 487. doi:10.1007/s11427-008-0068-y
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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 phsphatases structures are summarized.

Keywords

Ser/Thr phosphatasessubunit compositionsimilarities and differencescrystal structure

Copyright information

© Science in China Press and Springer-Verlag GmbH 2008

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiologyBeijing Normal University, Beijing Key LaboratoryBeijingChina
  2. 2.School of Life ScienceChangchun Normal UniversityChangchunChina