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PDBsum entry 5j8r
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References listed in PDB file
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Key reference
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Title
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Crystal structure and substrate specificity of ptpn12.
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Authors
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H.Li,
F.Yang,
C.Liu,
P.Xiao,
Y.Xu,
Z.Liang,
C.Liu,
H.Wang,
W.Wang,
W.Zheng,
W.Zhang,
X.Ma,
D.He,
X.Song,
F.Cui,
Z.Xu,
F.Yi,
J.P.Sun,
X.Yu.
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Ref.
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Cell Rep, 2016,
15,
1345-1358.
[DOI no: ]
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PubMed id
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Abstract
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PTPN12 is an important tumor suppressor that plays critical roles in various
physiological processes. However, the molecular basis underlying the substrate
specificity of PTPN12 remains uncertain. Here, enzymological and
crystallographic studies have enabled us to identify two distinct structural
features that are crucial determinants of PTPN12 substrate specificity: the pY+1
site binding pocket and specific basic charged residues along its surface loops.
Key structurally plastic regions and specific residues in PTPN12 enabled
recognition of different HER2 phosphorylation sites and regulated specific
PTPN12 functions. In addition, the structure of PTPN12 revealed a CDK2
phosphorylation site in a specific PTPN12 loop. Taken together, our results not
only provide the working mechanisms of PTPN12 for desphosphorylation of its
substrates but will also help in designing specific inhibitors of PTPN12.
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