期刊
NATURE STRUCTURAL BIOLOGY
卷 10, 期 2, 页码 115-119出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsb884
关键词
-
资金
- NCI NIH HHS [R01 CA073808, R01 CA073808-07] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008349] Funding Source: Medline
Cells produce proteases as inactive zymogens. Here, we demonstrate that this tactic can extend beyond proteases. By linking the N and C termini of ribonuclease A, we obstruct the active site with the amino acid sequence recognized by plasmepsin II, a highly specific protease from Plasmodium falciparum. We generate new N and C termini by circular permutation. In the presence of plasmepsin II, a ribonuclease zymogen gains similar to10(3)-fold in catalytic activity and maintains high conformational stability. We conclude that zymogen creation provides a new and versatile strategy for the control of enzymatic activity, as well as the potential development of chemotherapeutic agents.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据