Structure and catalytic mechanism of human protein tyrosine phosphatome

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초록

Together with protein tyrosine kinases (PTKs), protein tyrosine phosphatases (PTPs) serve as hallmarks in cellular signal transduction by controlling the reversible phosphorylation of 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, enabling us 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.

키워드

Classical PTPCrystal structureDual specificity PTPEyes absentProtein tyrosine phosphatase (PTP)CRYSTAL-STRUCTUREPHOSPHOINOSITIDE PHOSPHATASEEYES ABSENTDOMAINSPECIFICITYINSIGHTSACTIVATIONPRL-1PHOSPHORYLATIONRECOGNITION
제목
Structure and catalytic mechanism of human protein tyrosine phosphatome
저자
Kim, Seung JunRyu, Seong Eon
DOI
10.5483/BMBRep.2012.45.12.240
발행일
2012-12
유형
Review
저널명
BMB Reports
45
12
페이지
693 ~ 699

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