2esb

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spinqualitylabelsall models 2esb, resolution 2.Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of human DUSP18

Overview

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 approximately 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, A 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 beta-strands and participate, in extensive interactions with the catalytic domain, explaining the, thermostability of DSP18.

About this Structure

2ESB is a Single protein structure of sequence from Homo sapiens with ACT and EPE as ligands. Full crystallographic information is available from OCA.

Reference

Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family., Jeong DG, Cho YH, Yoon TS, Kim JH, Son JH, Ryu SE, Kim SJ, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):582-8. Epub 2006, May 12. PMID:16699184

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