Hsp90-Tau complex reveals molecular basis for specificity in chaperone action.
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ABSTRACT:
SUBMITTER: Karagoz GE
PROVIDER: S-EPMC4263503 | biostudies-literature | 2014 Feb
REPOSITORIES: biostudies-literature
Publications
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action.
Karagöz G Elif GE Duarte Afonso M S AM Akoury Elias E Ippel Hans H Biernat Jacek J Morán Luengo Tania T Radli Martina M Didenko Tatiana T Nordhues Bryce A BA Veprintsev Dmitry B DB Dickey Chad A CA Mandelkow Eckhard E Zweckstetter Markus M Boelens Rolf R Madl Tobias T Rüdiger Stefan G D SG
Cell 20140201 5
Protein folding in the cell relies on the orchestrated action of conserved families of molecular chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding path, yet the molecular basis of this timing is enigmatic, mainly because the substrate specificity of Hsp90 is poorly understood. Here, we obtained a structural model of Hsp90 in complex with its natural disease-associated substrate, the intrinsically disordered Tau protein. Hsp90 binds to a broad region in Tau t ...[more]
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