상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

The family-wide structure and function of human dual-specificity protein phosphatases

 

인간 이중특이성 탈인산화효소들의 구조와 기능

Authors 

Dae Gwin JeongC H WeiBonsu KuT J JeonP N ChienJ K KimS Y ParkH S HwangS Y RyuH ParkD S KimSeung Jun KimS E Ryu

Publisher 

International Union of Crystallography

Issue Date 

2014

Citation 

Acta Crystallographica. Section D, Biological Crystallography, vol. 70, no. D, pp. 421-435

Keywords 

dual-specificity protein phosphatasesDUSPsprotein tyrosine phosphatases

Abstract 

Dual-specificity protein phosphatases (DUSPs), which dephosphorylate both phosphoserine/threonine and phosphotyrosine, play vital roles in immune activation, brain function and cell-growth signalling. A family-wide structural library of human DUSPs was constructed based on experimental structure determination supplemented with homology modelling. The catalytic domain of each individual DUSP has characteristic features in the active site and in surface-charge distribution, indicating substrate-interaction specificity. The active-site loop-to-strand switch occurs in a subtype-specific manner, indicating that the switch process is necessary for characteristic substrate interactions in the corresponding DUSPs. A comprehensive analysis of the activity-inhibition profile and active-site geometry of DUSPs revealed a novel role of the active-pocket structure in the substrate specificity of DUSPs. A structure-based analysis of redox responses indicated that the additional cysteine residues are important for the protection of enzyme activity. The family-wide structures of DUSPs form a basis for the understanding of phosphorylation-mediated signal transduction and the development of therapeutics.

Citation 

Acta Crystallographica. Section D, Biological Crystallography, 70(D): 421-435

ISSN 

0907-4449

Link 

http://dx.doi.org/10.1107/S1399004713029866

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


Files in This Item: SizeFormat
12116.pdf2220KbAdobe PDF
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)