Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V
Dept of Biochem. and Mol. Biol. Jozef Stefan Institute, Ljubljana, Slovenia.
FEBS Lett. 1996 Apr 22;384(3):211-4. doi: 10.1016/0014-5793(96)00309-2.
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.
表达了野生型人组织蛋白酶B，其以两种晶体形式结晶，并在3.2和3.3埃分辨率下确定了其晶体结构。该结构表明，前肽在组织蛋白酶B表面折叠，保护酶活性位点不暴露于溶剂中。酶活性结构域的结构与天然酶的结构几乎相同[Musil等人（1991年），《欧洲分子生物学组织杂志》10，2321 - 2330]：主要区别在于封闭环残基高于成熟酶主体，支持前肽结构。
