%0 Journal Article
%A Kadavath, Harindranath
%A Jaremko, Mariusz
%A Jaremko, Lukasz
%A Biernat, Jacek
%A Mandelkow, Eckhard
%A Zweckstetter, Markus
%T Folding of the Tau Protein on Microtubules.
%J Angewandte Chemie / International edition
%V 54
%N 35
%@ 1433-7851
%C Weinheim
%I Wiley-VCH
%M DZNE-2020-04402
%P 10347-10351
%D 2015
%X 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.
%K Amyloid: chemistry
%K Humans
%K Magnetic Resonance Spectroscopy
%K Microtubules: chemistry
%K Protein Conformation
%K Protein Folding
%K tau Proteins: chemistry
%K Amyloid (NLM Chemicals)
%K tau Proteins (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:26094605
%R 10.1002/anie.201501714
%U https://pub.dzne.de/record/138080