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  Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90.

Oroz, J., Kim, J. H., Chang, B. J., & Zweckstetter, M. (2017). Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90. Nature Structural and Molecular Biology, 24(4), 407-413. doi:10.1038/nsmb.3380.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-E871-E Version Permalink: http://hdl.handle.net/21.11116/0000-0001-3BDC-6
Genre: Journal Article

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 Creators:
Oroz, J., Author
Kim, J. H., Author
Chang, B. J.1, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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 Abstract: The critical toxic species in over 40 human diseases are misfolded proteins. Their interaction with molecular chaperones such as Hsp90, which preferentially interacts with metastable proteins, is essential for the blocking of disease progression. Here we used nuclear magnetic resonance (NMR) spectroscopy to determine the three-dimensional structure of the misfolded cytotoxic monomer of the amyloidogenic human protein transthyretin, which is characterized by the release of the C-terminal β-strand and perturbations of the A-B loop. The misfolded transthyretin monomer, but not the wild-type protein, binds to human Hsp90. In the bound state, the Hsp90 dimer predominantly populates an open conformation, and transthyretin retains its globular structure. The interaction surface for the transthyretin monomer comprises the N-terminal and middle domains of Hsp90 and overlaps with that of the Alzheimer's-disease-related protein tau. Taken together, the data suggest that Hsp90 uses a mechanism for the recognition of aggregation-prone proteins that is largely distinct from those of other Hsp90 clients.

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Language(s): eng - English
 Dates: 2017-02-202017-04
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nsmb.3380
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 24 (4) Sequence Number: - Start / End Page: 407 - 413 Identifier: -