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

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 struc...

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Bibliographic Details
Published in:FEBS letters 1996-04, Vol.384 (3), p.211-214
Main Authors: Turk, D, Podobnik, M, Kuhelj, R, Dolinar, M, Turk, V
Format: Article
Language:English
Subjects:
Binding Sites
Cathepsin B - chemistry
Cathepsin B - metabolism
Crystallography, X-Ray
Cysteine Endopeptidases - chemistry
Cysteine Endopeptidases - metabolism
Enzyme Precursors - chemistry
Enzyme Precursors - metabolism
Humans
Models, Molecular
Papain - chemistry
Papain - metabolism
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Protein Conformation
Structure-Activity Relationship
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Summary: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.
ISSN:0014-5793