| pubmed-article:16537382 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16537382 | lifeskim:mentions | umls-concept:C0020289 | lld:lifeskim |
| pubmed-article:16537382 | lifeskim:mentions | umls-concept:C0041538 | lld:lifeskim |
| pubmed-article:16537382 | lifeskim:mentions | umls-concept:C1421309 | lld:lifeskim |
| pubmed-article:16537382 | lifeskim:mentions | umls-concept:C0678558 | lld:lifeskim |
| pubmed-article:16537382 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16537382 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:16537382 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:16537382 | pubmed:dateCreated | 2006-3-22 | lld:pubmed |
| pubmed-article:16537382 | pubmed:abstractText | The ubiquitin C-terminal hydrolase UCH-L1 (PGP9.5) comprises >1% of total brain protein but is almost absent from other tissues [Wilkinson, K. D., et al. (1989) Science 246, 670-673]. Mutations in the UCH-L1 gene have been reported to be linked to susceptibility to and protection from Parkinson's disease [Leroy, E., et al. (1998) Nature 395, 451-452; Maraganore, D. M., et al. (1999) Neurology 53, 1858-1860]. Abnormal overexpression of UCH-L1 has been shown to correlate with several forms of cancer [Hibi, K., et al. (1998) Cancer Res. 58, 5690-5694]. Because the amino acid sequence of UCH-L1 is similar to that of other ubiquitin C-terminal hydrolases, including the ubiquitously expressed UCH-L3, which appear to be unconnected to neurodegenerative disease, the structure of UCH-L1 and the effects of disease associated mutations on the structure and function are of considerable importance. We have determined the three-dimensional structure of human UCH-L1 at 2.4-A resolution by x-ray crystallography. The overall fold resembles that of other ubiquitin hydrolases, including UCH-L3, but there are a number of significant differences. In particular, the geometry of the catalytic residues in the active site of UCH-L1 is distorted in such a way that the hydrolytic activity would appear to be impossible without substrate induced conformational rearrangements. | lld:pubmed |
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| pubmed-article:16537382 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16537382 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16537382 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16537382 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:16537382 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:16537382 | pubmed:author | pubmed-author:PetskoGregory... | lld:pubmed |
| pubmed-article:16537382 | pubmed:author | pubmed-author:RingeDagmarD | lld:pubmed |
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| pubmed-article:16537382 | pubmed:author | pubmed-author:MerayRobin... | lld:pubmed |
| pubmed-article:16537382 | pubmed:author | pubmed-author:RaySoumya SSS | lld:pubmed |
| pubmed-article:16537382 | pubmed:author | pubmed-author:LuchanskySara... | lld:pubmed |
| pubmed-article:16537382 | pubmed:author | pubmed-author:LansburyPeter... | lld:pubmed |
| pubmed-article:16537382 | pubmed:author | pubmed-author:HoangQuyen... | lld:pubmed |
| pubmed-article:16537382 | pubmed:author | pubmed-author:KreinbringChe... | lld:pubmed |
| pubmed-article:16537382 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16537382 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:16537382 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:16537382 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16537382 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16537382 | pubmed:pagination | 4675-80 | lld:pubmed |
| pubmed-article:16537382 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16537382 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16537382 | pubmed:articleTitle | Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1. | lld:pubmed |
| pubmed-article:16537382 | pubmed:affiliation | Department of Chemistry and Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454-9110, USA. | lld:pubmed |
| pubmed-article:16537382 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16537382 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16537382 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16537382 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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