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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2007-8-16
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-10089417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-10222271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-10675325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-10712915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-10896920,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-11243894,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-11257442,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-11567148,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-14592767,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-14767517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-14998489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-15015494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-15034297,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-16014958,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-16166293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-16299534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-17055435,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-2153055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-7855884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-8051102,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-9847399,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-9857076,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17608567-9989501
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1545-7885
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e202
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17608567-Humans,
pubmed-meshheading:17608567-Animals,
pubmed-meshheading:17608567-Mice,
pubmed-meshheading:17608567-Crystallography, X-Ray,
pubmed-meshheading:17608567-Models, Molecular,
pubmed-meshheading:17608567-Protein Subunits,
pubmed-meshheading:17608567-Protein Conformation,
pubmed-meshheading:17608567-Amino Acid Sequence,
pubmed-meshheading:17608567-Protein Binding,
pubmed-meshheading:17608567-Simian virus 40,
pubmed-meshheading:17608567-Binding Sites,
pubmed-meshheading:17608567-Molecular Sequence Data,
pubmed-meshheading:17608567-Antigens, Viral, Tumor,
pubmed-meshheading:17608567-Sequence Alignment,
pubmed-meshheading:17608567-Protein Phosphatase 2
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