Structure and catalytic mechanism of human protein tyrosine phosphatome

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Title
Structure and catalytic mechanism of human protein tyrosine phosphatome
Author(s)
Seung Jun Kim; S E Ryu
Bibliographic Citation
BMB Reports, vol. 45, no. 12, pp. 693-699
Publication Year
2012
Abstract
Together with protein tyrosine kinases (PTKs), protein tyrosine phosphatases (PTPs) serve ashallmarks in cellular signal transduction by controlling the reversible phosphorylationof their substrates. The human genome is estimated to encode more than 100 PTPs, which can be divided into eleven sub-groups according to their structural and functional characteristics. All the crystal structures of catalytic domains of sub-groups have been elucidated, enablingus to understand their precise catalytic mechanism and to compare their structures across all sub-groups. In this review, I describe the structure and mechanism of catalytic domains of PTPs in the structural context.
Keyword
Classical PTPCrystal structureDual specificity PTPEyes absentProtein tyrosine phosphatase(PTP)
ISSN
1225-8687
Publisher
Korea Soc-Assoc-Inst
DOI
http://dx.doi.org/10.5483/BMBRep.2012.45.12.240
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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