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Journal Articles Protein Science Year : 2016

Remodeling of the conformational ensemble of the repeat domain of tau by an aggregation enhancer

Abstract

Misfolding of the microtubule-associated protein Tau is a hallmark of Alzheimer disease and several other neurodegenerative disorders. Because of the dynamic nature of the Tau protein, little is known however about the changes in Tau structure that occur during misfolding. Here we studied the structural consequences upon binding of the repeat domain of Tau, which plays a key role in pathogenic aggregation, to an aggregation enhancer. By combining NMR experiments with molecular simulations we show that binding of the aggregation enhancer polyglutamic acid remodels the conformational ensemble of Tau. Our study thus provides insight into an early event during misfolding of Tau. This article is protected by copyright. All rights reserved.

Dates and versions

hal-01299012 , version 1 (07-04-2016)

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Elias Akoury, Marco D. Mukrasch, Jacek Biernat, Katharina Tepper, Valéry Ozenne, et al.. Remodeling of the conformational ensemble of the repeat domain of tau by an aggregation enhancer. Protein Science, 2016, ⟨10.1002/pro.2911⟩. ⟨hal-01299012⟩
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