[논문]Structure and catalytic mechanism of human protein tyrosine phosphatome

Kim, Seung Jun; Ryu, Seong Eon

doi:10.5483/bmbrep.2012.45.12.240

Structure and catalytic mechanism of human protein tyrosine phosphatome 원문보기

BMB reports, v.45 no.12, 2012년, pp.693 - 699

Kim, Seung Jun (Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology) , Ryu, Seong Eon (Department of Bio Engineering, Hanyang University)

Abstract ▼ AI-Helper

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.

주제어

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문제 정의

As the structural information of the entitre sub-group of PTPs including eyes absent are available now, it is the right time to present a comprehensive review of the structure and mechanism of PTPome in terms of the three-dimensional structure. In this short review, we discuss a comparative analysis of our understanding of the catalytic domain of PTP structures and their mechanism.

가설 설정

The active site aspartate and magnesium ion are drawn as ball-and-stick models. (B) Catalytic mechanism of eyes absent. A proposed two-step catalytic mechanism for eyes absent is shown.

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