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  Folding of the Tau protein on microtubules.

Kadavath, H., Jaremko, M., Jaremko, L., Biernat, J., Mandelkow, E., & Zweckstetter, M. (2015). Folding of the Tau protein on microtubules. Angewandte Chemie International Edition, 54(35), 10347-10351. doi:10.1002/anie.201501714.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-7D75-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-3D1A-9
Genre: Journal Article

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 Creators:
Kadavath, H.1, Author              
Jaremko, M.2, Author              
Jaremko, L.2, Author              
Biernat, J., Author
Mandelkow, E., Author
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              

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Free keywords: Alzheimer’s disease;microtubules;NMR spectroscopy;structure elucidation;Tau protein
 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.

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Language(s): eng - English
 Dates: 2015-06-192015-08-24
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201501714
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 54 (35) Sequence Number: - Start / End Page: 10347 - 10351 Identifier: -