The crystal structure of DR6 in complex with the amyloid precursor protein provides insight into death receptor activation

被引：21

作者：

Xu, Kai ^{[1
]}

Olsen, Olav ^{[2
]}

Tzvetkova-Robev, Dorothea ^{[1
]}

Tessier-Lavigne, Marc ^{[2
]}

Nikolov, Dimitar B. ^{[1
]}

机构：

[1] Mem Sloan Kettering Canc Ctr, Struct Biol Program, New York, NY 10065 USA

[2] Rockefeller Univ, Lab Brain Dev & Repair, New York, NY 10065 USA

来源：

GENES & DEVELOPMENT | 2015年 / 29卷 / 08期

基金：

美国国家卫生研究院;

关键词：

amyloid precursor protein; crystal structure; death receptor 6; dimerization; signal activation; E2; DOMAIN; APP; HEPARIN; CONFORMATION; SECRETASE; REVEALS; DENSITY; PATHWAY; DIMER; E1;

D O I：

10.1101/gad.257675.114

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The amyloid precursor protein (APP) has garnered considerable attention due to its genetic links to Alzheimer's disease. Death receptor 6 (DR6) was recently shown to bind APP via the protein extracellular regions, stimulate axonal pruning, and inhibit synapse formation. Here, we report the crystal structure of the DR6 ectodomain in complex with the E2 domain of APP and show that it supports a model for APP-induced dimerization and activation of cell surface DR6.

引用

页码：785 / 790

页数：6

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