期刊
BIOLOGICAL CHEMISTRY
卷 398, 期 4, 页码 441-453出版社
WALTER DE GRUYTER GMBH
DOI: 10.1515/hsz-2016-0269
关键词
Alzheimer's disease; amyloid precursor protein; intramembrane protease; presenilin; transmembrane helix; gamma-secretase
资金
- Deutsche Forschungsgemeinschaft [LA699/ 4-1 (DL), LA699/20-1 (DL), STE847/4-1 (HS), FOR 2290]
- Bundesministerium fur Forschung und Technologie (KNDD) [01GI1004H]
- Center of Integrative Protein Science Munich (CIPSM)
- State of Bavaria
Intramembrane proteases comprise a number of different membrane proteins with different types of catalytic sites. Their common denominator is cleavage within the plane of the membrane, which usually results in peptide bond scission within the transmembrane helices of their substrates. Despite recent progress in the determination of high-resolution structures, as illustrated here for the gamma-secretase complex and its substrate C99, it is still unknown how these enzymes function and how they distinguish between substrates and non-substrates. In principle, substrate/non-substrate discrimination could occur at the level of substrate binding and/or cleavage. Focusing on the gamma-secretase/C99 pair, we will discuss recent observations suggesting that global motions within a substrate transmembrane helix may be much more important for defining a substrate than local unraveling at cleavage sites.
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