A wild-type human procathepsin B was expressed, crystallized in two crystal° forms and its crystal structure determined at 3.2 and 3.3 A 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 enzymaticaily 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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VeruKtP au, number 1, mb33l PEW% 098 IO Juns mt a IWWI, /"v&llriaI? ST Europenn Uia~haml~rsl !$wicttrr ~14~~~3~~1~~3. $0 ADBMIS ~t4~~$3~i~~~o~The complete amino mid sequence ~16" bovine cathepsin S and a partial sequence af baviaa cathepsin L protein and peptides were hydrolysed with 6 M I-ICI at 1lO'C for 24 and 72 h. Amino acid compositions were determined by using a Published by Eisevier Science Publishers B. V.A

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