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PDBsum entry 2esb
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References listed in PDB file
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Key reference
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Title
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Structure of human dsp18, A member of the dual-Specificity protein tyrosine phosphatase family.
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Authors
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D.G.Jeong,
Y.H.Cho,
T.S.Yoon,
J.H.Kim,
J.H.Son,
S.E.Ryu,
S.J.Kim.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2006,
62,
582-588.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 3.
Figure 3 Active site. (a) The difference electron-density map
for DSP18 was generated with the final model, omitting the bound
HEPES. The stereo map contoured at the 3.0  level
was presented as superposed with the refined model. The
hydrogen-bonding interactions around the active site are
represented by dashed lines. (b) Electrostatic potential
surfaces of DSP18 and VHR (PDB code [183]1vhr ) are presented.
Positive and negative potentials are coloured blue and red,
respectively. Residues near the active site are labelled.
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Figure 4.
Figure 4 CT motif. (a) The hydrophobic interactions between the
catalytic domain and the CT motif. The side chains of residues
involved in the hydrophobic interactions are represented and
labelled. Residues in the catalytic domain are coloured grey,
whereas those in the CT motif are coloured red. (b) Difference
F[o] - F[c] electron-density map around the CT motif omitted for
map calculation drawn in stereo with the refined model. The map
was contoured at a level of 3.0 .
Residues with atoms that participate in crystal contacts with
neighbours are coloured cyan.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
582-588)
copyright 2006.
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