title: 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.
abstract: 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.
authors.affiliation: Dept of Biochem. and Mol. Biol. Jozef Stefan Institute, Ljubljana, Slovenia.
authors.forename: D
authors.initials: D
authors.lastname: Turk
authors.forename: M
authors.initials: M
authors.lastname: Podobnik
authors.forename: R
authors.initials: R
authors.lastname: Kuhelj
authors.forename: M
authors.initials: M
authors.lastname: Dolinar
authors.forename: V
authors.initials: V
authors.lastname: Turk
mesh_terms: D001665:Binding Sites; D002401:Cathepsin B / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D004792:Enzyme Precursors / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D010206:Papain / Q000737:chemistry / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D004792:Enzyme Precursors; D010446:Peptide Fragments; D003546:Cysteine Endopeptidases; C057832:procathepsin B; D002401:Cathepsin B; D010206:Papain