TY  - JOUR
AU  - Kadavath, Harindranath
AU  - Jaremko, Mariusz
AU  - Jaremko, Lukasz
AU  - Biernat, Jacek
AU  - Mandelkow, Eckhard
AU  - Zweckstetter, Markus
TI  - Folding of the Tau Protein on Microtubules.
JO  - Angewandte Chemie / International edition
VL  - 54
IS  - 35
SN  - 1433-7851
CY  - Weinheim
PB  - Wiley-VCH
M1  - DZNE-2020-04402
SP  - 10347-10351
PY  - 2015
AB  - 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.
KW  - Amyloid: chemistry
KW  - Humans
KW  - Magnetic Resonance Spectroscopy
KW  - Microtubules: chemistry
KW  - Protein Conformation
KW  - Protein Folding
KW  - tau Proteins: chemistry
KW  - Amyloid (NLM Chemicals)
KW  - tau Proteins (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:26094605
DO  - DOI:10.1002/anie.201501714
UR  - https://pub.dzne.de/record/138080
ER  -