Cryo-EM structures of human γ-secretase

被引：16
|
作者：
Yang, Guanghui [1 ]
Zhou, Rui [1 ]
Shi, Yigong [1 ]
机构：
[1] Tsinghua Univ, Tsinghua Peking Joint Ctr Life Sci, Sch Life Sci, Beijing Adv Innovat Ctr Struct Biol, Beijing 100084, Peoples R China
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY | 2017年 / 46卷
基金：
中国国家自然科学基金;
关键词：
TERMINAL PAL MOTIF; AMYLOID PROTEIN; 3-DIMENSIONAL STRUCTURE; TRANSMEMBRANE DOMAIN-4; NICASTRIN FUNCTIONS; PRESENILIN-1; COMPLEX; PEN-2; MUTATIONS; COMPONENT;
D O I：
10.1016/j.sbi.2017.05.013
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：
gamma-secretase, a membrane-embedded aspartate protease, catalyzes peptide bond hydrolysis of a large variety of type I integral membrane proteins exemplified by amyloid precursor protein (APP). Cleavage of APP leads to formation of beta-amyloid plaque, which is a hallmark of Alzheimer's disease (AD). Over 200 AD-associated mutations are mapped to presenilin 1 (PS1), the catalytic component of gamma-secretase. In the past three years, several cryo-electron microscopy (cryo-EM) structures of human gamma-secretase have been determined at near atomic resolutions. Here we summarize the methods involved and discuss structural features of gamma-secretase and the associated functional insights.
引用
收藏
页码：55 / 64
页数：10
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