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PDBsum entry 4hjp
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References listed in PDB file
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Key reference
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Title
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Shp family protein tyrosine phosphatases adopt canonical active-Site conformations in the apo and phosphate-Bound states.
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Authors
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N.L.Alicea-Velazquez,
T.J.Boggon.
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Ref.
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Protein Pept Lett, 2013,
20,
1039-1048.
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PubMed id
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Abstract
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Protein tyrosine phosphatase (PTP) catalytic domains undergo a series of
conformational changes in order to mediate dephosphorylation of their tyrosine
phosphorylated substrates. An important conformational change occurs in the
Tryptophan-Proline-Aspartic acid (WPD) loop, which contains the conserved
catalytic aspartate. Upon substrate binding, the WPD loop transitions from the
'open' to the 'closed' state, thus allowing optimal positioning of the catalytic
aspartate for substrate dephosphorylation. The dynamics of WPD loop
conformational changes have previously been studied for PTP1B, HePTP, and the
bacterial phosphatase YopH, but have not yet been comprehensively studied for
the nonreceptor tyrosine phosphatase SHP-1 (PTPN6). To structurally describe the
changes in WPD loop conformation in SHP-1, we have determined the 1.4 Å crystal
structure of the catalytic domain of SHP-1 in the Apo state and the 1.8 Å
crystal structure of the SHP-1 catalytic domain in complex with a phosphate ion.
We provide structural analysis for the WPD loop closed state of SHP phosphatases
and the conformational changes that occur upon WPD loop closure.
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