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Title: Domain swapping in p13suc1 results in formation of native-like, cytotoxic aggregates
Authors: Rousseau, Frederic ×
Wilkinson, Hannah
Villanueva, Josep
Serrano, Luis
Schymkowitz, Joost
Itzhaki, Laura S #
Issue Date: Oct-2006
Publisher: Academic Press
Series Title: Journal of Molecular Biology vol:363 issue:2 pages:496-505
Abstract: The field of protein aggregation has been occupied mainly with the study of beta-strand self-association that occurs as a result of misfolding and leads to the formation of toxic protein aggregates and amyloid fibers. However, some of these aggregates retain native-like structural and enzymatic properties suggesting mechanisms other than beta-strand assembly. p13suc1 is a small protein that can exist as a monomer or a domain-swapped dimer. Here, we show that, under native conditions, p13suc1 forms three-dimensional domain-swapped aggregates, and that these aggregates are cytotoxic. Thus, toxicity of protein aggregates is not only associated with beta-rich assemblies and amyloid fibers, involving non-native interactions, but it can be induced by oligomeric misassembly that maintains predominantly native-like interactions. (c) 2006 Elsevier Ltd. All rights reserved.
URI: 
ISSN: 0022-2836
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Non-KU Leuven Association publications
× corresponding author
# (joint) last author

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