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PDBsum entry 2pf4
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Hydrolase regulator/viral protein
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PDB id
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2pf4
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Contents |
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575 a.a.
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163 a.a.
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152 a.a.
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142 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural basis of pp2a inhibition by small t antigen.
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Authors
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U.S.Cho,
S.Morrone,
A.A.Sablina,
J.D.Arroyo,
W.C.Hahn,
W.Xu.
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Ref.
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Plos Biol, 2007,
5,
e202.
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PubMed id
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Abstract
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The SV40 small t antigen (ST) is a potent oncoprotein that perturbs the function
of protein phosphatase 2A (PP2A). ST directly interacts with the PP2A
scaffolding A subunit and alters PP2A activity by displacing regulatory B
subunits from the A subunit. We have determined the crystal structure of
full-length ST in complex with PP2A A subunit at 3.1 A resolution. ST consists
of an N-terminal J domain and a C-terminal unique domain that contains two
zinc-binding motifs. Both the J domain and second zinc-binding motif interact
with the intra-HEAT-repeat loops of HEAT repeats 3-7 of the A subunit, which
overlaps with the binding site of the PP2A B56 subunit. Intriguingly, the first
zinc-binding motif is in a position that may allow it to directly interact with
and inhibit the phosphatase activity of the PP2A catalytic C subunit. These
observations provide a structural basis for understanding the oncogenic
functions of ST.
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