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Angew Chem Int Ed Engl. 2015 Aug 24;54(35):10347-51. doi: 10.1002/anie.201501714. Epub 2015 Jun 19.

Folding of the Tau Protein on Microtubules.

Author information

  • 1Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen (Germany).
  • 2Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Göttingen (Germany).
  • 3Center for the Molecular Physiology of the Brain, University Medical Center, Göttingen (Germany).
  • 4Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE) & CAESAR Research Center, Ludwig-Erhard-Allee 2, Bonn (Germany).
  • 5Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen (Germany). markus.zweckstetter@dzne.de.
  • 6Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Göttingen (Germany). markus.zweckstetter@dzne.de.
  • 7Center for the Molecular Physiology of the Brain, University Medical Center, Göttingen (Germany). markus.zweckstetter@dzne.de.

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.

KEYWORDS:

Alzheimer’s disease; NMR spectroscopy; Tau protein; microtubules; structure elucidation

PMID:
26094605
DOI:
10.1002/anie.201501714
[PubMed - indexed for MEDLINE]
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