English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Hsp90-Tau complex reveals molecular basis for specificity in chaperone action.

Karagoz, G. E., Duarte, A. M. S., Akoury, E., Ippel, H., Biernat, J., Luengo, T. M., et al. (2014). Hsp90-Tau complex reveals molecular basis for specificity in chaperone action. Cell, 156(5), 963-974. doi:10.1016/j.cell.2014.01.037.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-F4C3-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CC43-0
Genre: Journal Article

Files

show Files
hide Files
:
2007877.pdf (Publisher version), 3MB
Name:
2007877.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2007877_Suppl_1.pdf (Supplementary material), 234KB
Name:
2007877_Suppl_1.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2007877_Suppl_2.pdf (Supplementary material), 4MB
Name:
2007877_Suppl_2.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Karagoz, G. E., Author
Duarte, A. M. S., Author
Akoury, E.1, Author              
Ippel, H., Author
Biernat, J., Author
Luengo, T. M., Author
Radli, M., Author
Didenko, T., Author
Nordhues, B. A., Author
Veprintsev, D. B., Author
Dickey, C. A., Author
Mandelkow, E., Author
Zweckstetter, M.1, Author              
Boelens, R., Author
Madl, T., Author
Rudiger, S. G. D., Author
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

Content

show
hide
Free keywords: Paired helical filaments; Escherichia-coli Hsp90; N-terminal domain; X-ray-scattering; NMR-spectroscopy; Tau-protein; Crystal-structure; Structural-analysis; Intrinsic disorder; Quality-control
 Abstract: 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 that includes the aggregation-prone repeats. Complementarily, a 106-angstrom-long substrate-binding interface in Hsp90 enables many low-affinity contacts. This allows recognition of scattered hydrophobic residues in late folding intermediates that remain after early burial of the Hsp70 sites. Our model resolves the paradox of how Hsp90 specifically selects for late folding intermediates but also for some intrinsically disordered proteins-through the eyes of Hsp90 they look the same.

Details

show
hide
Language(s): eng - English
 Dates: 2014-02-27
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.cell.2014.01.037
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Cell
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 156 (5) Sequence Number: - Start / End Page: 963 - 974 Identifier: -