Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain‐like cysteine protease and its propeptide

FEBS Letters

Podobnik, Marjeta¹  Dolinar, Marko¹  Turk, Dušan¹  Kuhelj, Robert¹  Turk, Vito¹ 

[1] Dept. of Biochem. and Mol. Biol., Jozef Stefan Institute, Jamova 39, 61111 Ljubljana, Slovenia

关键词: Cathepsin B;    Cysteine protease;    Proenzyme;    Crystal structure;    Papain;    RMS;    root mean square;    PEG;    polyethylene glycol;   

DOI  :  10.1016/0014-5793(96)00309-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A wild-type human procathepsin B was expressed, crystallized in two crystal forms and its crystal structure determined at 3.2 and 3.3 Å 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.

【 授权许可】

Unknown