| pubmed-article:17608567 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17608567 | lifeskim:mentions | umls-concept:C1704708 | lld:lifeskim |
| pubmed-article:17608567 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:17608567 | lifeskim:mentions | umls-concept:C0255156 | lld:lifeskim |
| pubmed-article:17608567 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:17608567 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17608567 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:17608567 | lifeskim:mentions | umls-concept:C0037352 | lld:lifeskim |
| pubmed-article:17608567 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:17608567 | pubmed:dateCreated | 2007-8-16 | lld:pubmed |
| pubmed-article:17608567 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17608567 | 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. | lld:pubmed |
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| pubmed-article:17608567 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17608567 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17608567 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17608567 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17608567 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:17608567 | pubmed:issn | 1545-7885 | lld:pubmed |
| pubmed-article:17608567 | pubmed:author | pubmed-author:HahnWilliam... | lld:pubmed |
| pubmed-article:17608567 | pubmed:author | pubmed-author:XuWenqingW | lld:pubmed |
| pubmed-article:17608567 | pubmed:author | pubmed-author:ArroyoJason... | lld:pubmed |
| pubmed-article:17608567 | pubmed:author | pubmed-author:SablinaAnna... | lld:pubmed |
| pubmed-article:17608567 | pubmed:author | pubmed-author:ChoUhn SooUS | lld:pubmed |
| pubmed-article:17608567 | pubmed:author | pubmed-author:MorroneSeamus... | lld:pubmed |
| pubmed-article:17608567 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17608567 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:17608567 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17608567 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17608567 | pubmed:pagination | e202 | lld:pubmed |
| pubmed-article:17608567 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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