| pubmed-article:15531586 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15531586 | lifeskim:mentions | umls-concept:C0038661 | lld:lifeskim |
| pubmed-article:15531586 | lifeskim:mentions | umls-concept:C0020289 | lld:lifeskim |
| pubmed-article:15531586 | lifeskim:mentions | umls-concept:C0041538 | lld:lifeskim |
| pubmed-article:15531586 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:15531586 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15531586 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:15531586 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:15531586 | pubmed:dateCreated | 2005-1-11 | lld:pubmed |
| pubmed-article:15531586 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15531586 | pubmed:abstractText | Ubiquitin C-terminal hydrolases (UCHs) comprise a family of small ubiquitin-specific proteases of uncertain function. Although no cellular substrates have been identified for UCHs, their highly tissue-specific expression patterns and the association of UCH-L1 mutations with human disease strongly suggest a critical role. The structure of the yeast UCH Yuh1-ubiquitin aldehyde complex identified an active site crossover loop predicted to limit the size of suitable substrates. We report the 1.45 A resolution crystal structure of human UCH-L3 in complex with the inhibitor ubiquitin vinylmethylester, an inhibitor that forms a covalent adduct with the active site cysteine of ubiquitin-specific proteases. This structure confirms the predicted mechanism of the inhibitor and allows the direct comparison of a UCH family enzyme in the free and ligand-bound state. We also show the efficient hydrolysis by human UCH-L3 of a 13-residue peptide in isopeptide linkage with ubiquitin, consistent with considerable flexibility in UCH substrate size. We propose a model for the catalytic cycle of UCH family members which accounts for the hydrolysis of larger ubiquitin conjugates. | lld:pubmed |
| pubmed-article:15531586 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15531586 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15531586 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15531586 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15531586 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15531586 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:15531586 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15531586 | pubmed:author | pubmed-author:PloeghHidde... | lld:pubmed |
| pubmed-article:15531586 | pubmed:author | pubmed-author:GaudetRachell... | lld:pubmed |
| pubmed-article:15531586 | pubmed:author | pubmed-author:OvaaHuibH | lld:pubmed |
| pubmed-article:15531586 | pubmed:author | pubmed-author:GalardyPaul... | lld:pubmed |
| pubmed-article:15531586 | pubmed:author | pubmed-author:MeesterWim... | lld:pubmed |
| pubmed-article:15531586 | pubmed:author | pubmed-author:MisaghiShahra... | lld:pubmed |
| pubmed-article:15531586 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15531586 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:15531586 | pubmed:volume | 280 | lld:pubmed |
| pubmed-article:15531586 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15531586 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15531586 | pubmed:pagination | 1512-20 | lld:pubmed |
| pubmed-article:15531586 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:15531586 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15531586 | pubmed:articleTitle | Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate. | lld:pubmed |
| pubmed-article:15531586 | pubmed:affiliation | Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA. | lld:pubmed |
| pubmed-article:15531586 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15531586 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15531586 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:15531586 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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