Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family = 인간 이중특이성 탈인산화효소 DSP18의 구조

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Title
Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family = 인간 이중특이성 탈인산화효소 DSP18의 구조
Author(s)
Dae Gwin Jeong; Y H Cho; Tae-Sung Yoon; J H Kim; Jeong Hee Son; Seong Eon Ryu; Seung Jun Kim
Bibliographic Citation
Acta Crystallographica Section D-Biological Crystallography, vol. D62, no. 6, pp. 582-588
Publication Year
2006
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.
ISSN
0907-4449
Publisher
Int Union Crystallography
DOI
http://dx.doi.org/10.1107/S0907444906010109
Type
Article
Appears in Collections:
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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