000138080 001__ 138080 000138080 005__ 20240321220351.0 000138080 0247_ $$2doi$$a10.1002/anie.201501714 000138080 0247_ $$2pmid$$apmid:26094605 000138080 0247_ $$2ISSN$$a0044-8249 000138080 0247_ $$2ISSN$$a0570-0833 000138080 0247_ $$2ISSN$$a1433-7851 000138080 0247_ $$2ISSN$$a1521-3757 000138080 0247_ $$2ISSN$$a1521-3773 000138080 0247_ $$2altmetric$$aaltmetric:4191614 000138080 037__ $$aDZNE-2020-04402 000138080 041__ $$aEnglish 000138080 082__ $$a540 000138080 1001_ $$0P:(DE-2719)2811307$$aKadavath, Harindranath$$b0$$eFirst author$$udzne 000138080 245__ $$aFolding of the Tau Protein on Microtubules. 000138080 260__ $$aWeinheim$$bWiley-VCH$$c2015 000138080 264_1 $$2Crossref$$3online$$bWiley$$c2015-06-19 000138080 264_1 $$2Crossref$$3print$$bWiley$$c2015-08-24 000138080 3367_ $$2DRIVER$$aarticle 000138080 3367_ $$2DataCite$$aOutput Types/Journal article 000138080 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1685112497_10310 000138080 3367_ $$2BibTeX$$aARTICLE 000138080 3367_ $$2ORCID$$aJOURNAL_ARTICLE 000138080 3367_ $$00$$2EndNote$$aJournal Article 000138080 520__ $$aMicrotubules 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. 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