Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state

The BRICHOS domain is a chaperone that can act against amyloid-β peptide fibril formation and non-fibrillar protein aggregation. Here the authors use a multidisciplinary approach and show that the Bri2 BRICHOS domain has qualitatively different chaperone activities depending on its quaternary struct...

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Bibliographic Details
Main Authors: Gefei Chen, Axel Abelein, Harriet E. Nilsson, Axel Leppert, Yuniesky Andrade-Talavera, Simone Tambaro, Lovisa Hemmingsson, Firoz Roshan, Michael Landreh, Henrik Biverstål, Philip J. B. Koeck, Jenny Presto, Hans Hebert, André Fisahn, Jan Johansson
Format: Article
Language:English
Published: Nature Publishing Group 2017-12-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-02056-4
Description
Summary:The BRICHOS domain is a chaperone that can act against amyloid-β peptide fibril formation and non-fibrillar protein aggregation. Here the authors use a multidisciplinary approach and show that the Bri2 BRICHOS domain has qualitatively different chaperone activities depending on its quaternary structure.
ISSN:2041-1723