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Title 

Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family

 

인간 이중특이성 탈인산화효소 DSP18의 구조

Authors 

Dae Gwin JeongY H ChoTae-Sung YoonJ H KimJeong Hee SonSeong Eon RyuSeung Jun Kim

Publisher 

International Union of Crystallography

Issue Date 

2006

Citation 

Acta Crystallographica. Section D, Biological Crystallography, vol. D62, no. 6, pp. 582-588

Keywords 

DSP18 protein, humanprotein tyrosine phosphataseamino acid sequencechemical structureclassificationenzyme active sitehumanmolecular geneticsprotein motifsequence alignment

Abstract 

The human dual-specificity protein phosphatase 18 (DSP18) gene and its protein product have recently been characterized. Like most DSPs, DSP18 displays dephosphorylating activity towards both phosphotyrosine and phosphothreonine residues. However, DSP18 is distinct from other known DSPs in terms of the existence of ∼30 residues at the C-terminus of the catalytic domain and an unusual optimum activity profile at 328 K. The crystal structure of human DSP18 has been determined at 2.0 ? resolution. The catalytic domain of DSP18 adopts a fold similar to that known for other DSP structures. Although good alignments are found with other DSPs, substantial differences are also found in the regions surrounding the active site, suggesting that DSP18 constitutes a unique structure with a distinct substrate specificity. Furthermore, the residues at the C-terminus fold into two antiparallel β-strands and participate in extensive interactions with the catalytic domain, explaining the thermostability of DSP18.

Citation 

Acta Crystallographica. Section D, Biological Crystallography, D62(6): 582-588

ISSN 

0907-4449

Link 

http://dx.doi.org/10.1107/S0907444906010109

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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