| pubmed-article:2143562 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2143562 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2143562 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:2143562 | lifeskim:mentions | umls-concept:C0332255 | lld:lifeskim |
| pubmed-article:2143562 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2143562 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:2143562 | pubmed:issue | 6285 | lld:pubmed |
| pubmed-article:2143562 | pubmed:dateCreated | 1990-9-17 | lld:pubmed |
| pubmed-article:2143562 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2143562 | pubmed:abstractText | The three-dimensional structure of the amino-terminal 44K ATPase fragment of the 70K bovine heat-shock cognate protein has been solved to a resolution of 2.2 A. The ATPase fragment has two structural lobes with a deep cleft between them; ATP binds at the base of the cleft. Surprisingly, the nucleotide-binding 'core' of the ATPase fragment has a tertiary structure similar to that of hexokinase, although the remainder of the structures of the two proteins are completely dissimilar, suggesting that both the phosphotransferase mechanism and the substrate-induced conformational change intrinsic to the hexokinases may be used by the 70K heat shock-related proteins. | lld:pubmed |
| pubmed-article:2143562 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2143562 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2143562 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2143562 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2143562 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2143562 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:2143562 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:2143562 | pubmed:author | pubmed-author:McKayD BDB | lld:pubmed |
| pubmed-article:2143562 | pubmed:author | pubmed-author:FlahertyK MKM | lld:pubmed |
| pubmed-article:2143562 | pubmed:author | pubmed-author:DeLuca-Flaher... | lld:pubmed |
| pubmed-article:2143562 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2143562 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:2143562 | pubmed:volume | 346 | lld:pubmed |
| pubmed-article:2143562 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2143562 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2143562 | pubmed:pagination | 623-8 | lld:pubmed |
| pubmed-article:2143562 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:2143562 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2143562 | pubmed:articleTitle | Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. | lld:pubmed |
| pubmed-article:2143562 | pubmed:affiliation | Beckman Laboratories for Structural Biology, Department of Cell Biology, Stanford University School of Medicine, California 94305-5400. | lld:pubmed |
| pubmed-article:2143562 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2143562 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2143562 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2143562 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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