English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Dynamic Aha1 co-chaperone binding to human Hsp90.

Oroz, J., Blair, L. J., & Zweckstetter, M. (2019). Dynamic Aha1 co-chaperone binding to human Hsp90. Protein Science, (in press). doi:10.1002/pro.3678.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0004-41CC-D Version Permalink: http://hdl.handle.net/21.11116/0000-0004-41D0-7
Genre: Journal Article

Files

show Files
hide Files
:
3135986.pdf (Preprint), 4MB
 
File Permalink:
-
Name:
3135986.pdf
Description:
-
Visibility:
Restricted ( Max Planck Society (every institute); )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
3135986_Suppl.pdf (Supplementary material), 3MB
Name:
3135986_Suppl.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Oroz, J., Author
Blair, L. J., Author
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

Content

show
hide
Free keywords: Aha1 ; Hsp90 ; allostery ; co-chaperone ; structure
 Abstract: Hsp90 is an essential chaperone that requires large allosteric changes to determine its ATPase activity and client binding. The co-chaperone Aha1, which is the major ATPase stimulator in eukaryotes, is important for regulation of Hsp90's allosteric timing. Little is known, however, about the structure of the Hsp90/Aha1 complex. Here, we characterize the solution structure of unmodified human Hsp90/Aha1 complex using NMR spectroscopy. We show that the 214-kDa complex forms by a two-step binding mechanism and adopts multiple conformations in the absence of nucleotide. Aha1 induces structural changes near Hsp90's nucleotide-binding site, providing a basis for its ATPase-enhancing activity. Our data reveal important aspects of this pivotal chaperone/co-chaperone interaction and emphasize the relevance of characterizing dynamic chaperone structures in solution.

Details

show
hide
Language(s): eng - English
 Dates: 2019-07-12
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/pro.3678
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Protein Science
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: - Sequence Number: (in press) Start / End Page: - Identifier: -