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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1996-6-13
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pubmed:abstractText |
A wild-type human procathepsin B was expressed, crystallized in two crystal forms and its crystal structure determined at 3.2 and 3.3 Angstroms resolution. The structure reveals that the propeptide folds on the cathepsin B surface, shielding the enzyme active site from exposure to solvent. The structure of the enzymatically active domains is virtually identical to that of the native enzyme [Musil et al. (1991) EMBO J. 10, 2321-2330]: the main difference is that the occluding loop residues are lifted above the body of the mature enzyme, supporting the propeptide structure.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
22
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|
pubmed:volume |
384
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
211-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8617355-Binding Sites,
pubmed-meshheading:8617355-Cathepsin B,
pubmed-meshheading:8617355-Crystallography, X-Ray,
pubmed-meshheading:8617355-Cysteine Endopeptidases,
pubmed-meshheading:8617355-Enzyme Precursors,
pubmed-meshheading:8617355-Humans,
pubmed-meshheading:8617355-Models, Molecular,
pubmed-meshheading:8617355-Papain,
pubmed-meshheading:8617355-Peptide Fragments,
pubmed-meshheading:8617355-Protein Conformation,
pubmed-meshheading:8617355-Structure-Activity Relationship
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pubmed:year |
1996
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pubmed:articleTitle |
Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide.
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pubmed:affiliation |
Dept of Biochem. and Mol. Biol. Jozef Stefan Institute, Ljubljana, Slovenia.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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