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  Burial of the polymorphic residue 129 in amyloid fibrils of prion stop mutants.

Skora, L., Fonseca, L., Hofele, R. V., Riedel, D., Giller, K., Watzlawik, J., et al. (2013). Burial of the polymorphic residue 129 in amyloid fibrils of prion stop mutants. Journal of Biological Chemistry, 288(5), 2994-3002. doi:10.1074/jbc.M112.423715 jbc.M112.423715.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8FBF-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CF61-1
Genre: Journal Article

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 Creators:
Skora, L.1, Author              
Fonseca, L.1, Author              
Hofele, R. V.2, Author              
Riedel, D.3, Author              
Giller, K.4, Author              
Watzlawik, J., Author
Schulz-Schaeffer, W. J., Author
Urlaub, H.2, Author              
Becker, S.4, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck SOciety, ou_578613              
3Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              
4Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: Prions, amyloid, NMR, mass spectrometry, aggregation
 Abstract: Misfolding of the natively alpha-helical prion protein into a beta-sheet rich isoform is related to various human diseases such as Creutzfeldt-Jakob disease and Gerstmann-Straeussler-Scheinker-like syndrome. In humans the disease phenotype is modified by a methionine/valine polymorphism at codon 129 of the prion protein gene. Using a combination of H/D exchange coupled to NMR spectroscopy, hydroxyl radical probing detected by mass spectrometry and site-directed mutagenesis we demonstrate that stop mutants of the human prion protein have a conserved amyloid core. The 129 residue is deeply buried in the amyloid core structure and its mutation strongly impacts aggregation. Taken together the data support a critical role of the polymorphic residue 129 of the human prion protein in aggregation and disease.

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Language(s): eng - English
 Dates: 2013-02-01
 Publication Status: Published online
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 Table of Contents: -
 Rev. Method: Peer
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 288 (5) Sequence Number: - Start / End Page: 2994 - 3002 Identifier: -