Folding of the Tau Protein on Microtubules |
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| Authors: | Dr. Harindranath Kadavath Dr. Mariusz Jaremko Dr. Łukasz Jaremko Dr. Jacek Biernat Prof. Dr. Eckhard Mandelkow Prof. Dr. Markus Zweckstetter |
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| Affiliation: | 1. Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G?ttingen (Germany);2. Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), G?ttingen (Germany);3. Center for the Molecular Physiology of the Brain, University Medical Center, G?ttingen (Germany);4. Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE) & CAESAR Research Center, Ludwig‐Erhard‐Allee 2, Bonn (Germany) |
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| 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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| Keywords: | Alzheimer’ s disease microtubules NMR spectroscopy structure elucidation Tau protein |
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