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

被引：136

作者：

Turk, D ^{[1
]}

Podobnik, M ^{[1
]}

Kuhelj, R ^{[1
]}

Dolinar, M ^{[1
]}

Turk, V ^{[1
]}

机构：

[1] MAX PLANCK INST BIOCHEM, D-82152 MARTINSRIED, GERMANY

来源：

FEBS LETTERS | 1996年 / 384卷 / 03期

关键词：

cathepsin B; cysteine protease; proenzyme; crystal structure; papain;

D O I：

10.1016/0014-5793(96)00309-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 Angstrom 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 [Mush 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.

引用

页码：211 / 214

页数：4