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

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.
Authors:
 [1] ;  [2] ;  [1] ;  [2] ;  [1]
  1. Memorial Sloan-Kettering Cancer Center, New York, NY (United States). Structural Biology Program
  2. Rockefeller Univ., New York, NY (United States). Lab. of Brain Development and Repair
Publication Date:
OSTI Identifier:
1178473
Grant/Contract Number:
AC02-06CH11357; 1R01NS089786; P41 GM103403
Type:
Accepted Manuscript
Journal Name:
Genes and Development
Additional Journal Information:
Journal Volume: 29; Journal Issue: 8; Journal ID: ISSN 0890-9369
Publisher:
Cold Springs Harbor Press
Research Org:
Memorial Sloan-Kettering Cancer Center, New York, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC); National Inst. of Health (NIH) (United States)
Contributing Orgs:
Rockefeller Univ., New York, NY (United States)
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; amyloid precursor protein; crystal structure; death receptor 6; dimerization; signal activation