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    FEBS Lett. 1996 Apr 22;384(3):211-4.

    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.

    Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V.

    Dept of Biochem. and Mol. Biol. Jozef Stefan Institute, Ljubljana, Slovenia.

    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.

    PMID: 8617355 [PubMed - indexed for MEDLINE]

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