期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 37, 期 -, 页码 97-107出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2015.12.008
关键词
-
资金
- National Natural Science Foundation of China [31130002, 31321062]
- postdoctoral foundation of the Center for Life Sciences
- Gordon and Betty Moore Foundation Fellow of the Life Sciences Research Foundation
Intramembrane proteases catalyze hydrolysis of peptide bond within the lipid bilayer and play a key role in a variety of cellular processes. These membrane-embedded enzymes comprise four major classes: rhomboid serine proteases, site-2 metalloproteases, Rce1-type glutamyl proteases, and aspartyl proteases exemplified by signal peptide peptidase and gamma-secretase. In the past several years, three-dimensional structures of representative members of these four classes of intramembrane protease have been reported at atomic resolutions, which reveal distinct protein folds and active site configurations. These structures, together with structure guided biochemical analyses, shed light on the working mechanisms of water access and substrate entry. In this review, we discuss the shared as well as unique features of these intramembrane proteases, with a focus on presenilin the catalytic component of gamma-secretase.
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