期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 54, 期 35, 页码 10347-10351出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201501714
关键词
Alzheimer's disease; microtubules; NMR spectroscopy; structure elucidation; Tau protein
资金
- MPG consortium Toxic Protein Conformation
- Wellcome Trust
- Foundation for Polish Science START
- Ventures Programme - EU European Regional Development Fund
- Deutsche Forschungsgemeinschaft [ZW 71/8-1]
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 beta-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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