Abstract
Microtubules are regulated by microtubule-associated proteins. However, little is known about the structure of microtubule-associated proteins in complex with microtubules. Herein we show that the microtubule-associated protein Tau, which is intrinsically disordered in solution, locally folds into a stable structure upon binding to microtubules. While Tau is highly flexible in solution and adopts a β-sheet structure in amyloid fibrils, in complex with microtubules the conserved hexapeptides at the beginning of the Tau repeats two and three convert into a hairpin conformation. Thus, binding to microtubules stabilizes a unique conformation in Tau.
Original language | English (US) |
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Pages (from-to) | 10347-10351 |
Number of pages | 5 |
Journal | Angewandte Chemie - International Edition |
Volume | 54 |
Issue number | 35 |
DOIs | |
State | Published - Aug 1 2015 |
Externally published | Yes |
Bibliographical note
Publisher Copyright:© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Keywords
- Alzheimer's disease
- NMR spectroscopy
- Tau protein
- microtubules
- structure elucidation
ASJC Scopus subject areas
- Catalysis
- General Chemistry