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| pubmed-article:15039704 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
| pubmed-article:15039704 | lifeskim:mentions | umls-concept:C0243044 | lld:lifeskim |
| pubmed-article:15039704 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:15039704 | lifeskim:mentions | umls-concept:C0337076 | lld:lifeskim |
| pubmed-article:15039704 | lifeskim:mentions | umls-concept:C1412886 | lld:lifeskim |
| pubmed-article:15039704 | lifeskim:mentions | umls-concept:C1825534 | lld:lifeskim |
| pubmed-article:15039704 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15039704 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:15039704 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:15039704 | pubmed:dateCreated | 2004-3-24 | lld:pubmed |
| pubmed-article:15039704 | pubmed:abstractText | Hsp90 is a molecular chaperone essential for the activation and assembly of many key eukaryotic signalling and regulatory proteins. Hsp90 is assisted and regulated by co-chaperones that participate in an ordered series of dynamic multiprotein complexes, linked to Hsp90 conformationally coupled ATPase cycle. The co-chaperones Aha1 and Hch1 bind to Hsp90 and stimulate its ATPase activity. Biochemical analysis shows that this activity is dependent on the N-terminal domain of Aha1, which interacts with the central segment of Hsp90. The structural basis for this interaction is revealed by the crystal structure of the N-terminal domain (1-153) of Aha1 (equivalent to the whole of Hch1) in complex with the middle segment of Hsp90 (273-530). Structural analysis and mutagenesis show that binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone. | lld:pubmed |
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| pubmed-article:15039704 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15039704 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15039704 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15039704 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:15039704 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:15039704 | pubmed:author | pubmed-author:DruMM | lld:pubmed |
| pubmed-article:15039704 | pubmed:author | pubmed-author:PearlLaurence... | lld:pubmed |
| pubmed-article:15039704 | pubmed:author | pubmed-author:PiperPeter... | lld:pubmed |
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| pubmed-article:15039704 | pubmed:author | pubmed-author:RoeS MarkSM | lld:pubmed |
| pubmed-article:15039704 | pubmed:author | pubmed-author:LiaoChunyanC | lld:pubmed |
| pubmed-article:15039704 | pubmed:author | pubmed-author:VlasicIgnacij... | lld:pubmed |
| pubmed-article:15039704 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15039704 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:15039704 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:15039704 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15039704 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15039704 | pubmed:pagination | 1402-10 | lld:pubmed |
| pubmed-article:15039704 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15039704 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15039704 | pubmed:articleTitle | Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. | lld:pubmed |
| pubmed-article:15039704 | pubmed:affiliation | Chester Beatty Laboratories, Section of Structural Biology, The Institute of Cancer Research, London, UK. | lld:pubmed |
| pubmed-article:15039704 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15039704 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15039704 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:15039704 | pubmed:publicationType | Corrected and Republished Article | lld:pubmed |
| pubmed-article:15039704 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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