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  Comparison of the 3D structures of mouse and human alpha-synuclein fibrils by it solid-state NMR and STEM.

Hwang, S., Fricke, P., Zinke, M., Giller, K., Wall, J. S., Riedel, D., et al. (2019). Comparison of the 3D structures of mouse and human alpha-synuclein fibrils by it solid-state NMR and STEM. Journal of Structural Biology, 206(1), 43-48. doi:10.1016/j.jsb.2018.04.003.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-84F8-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-84FC-C
Genre: Journal Article

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 Creators:
Hwang, S., Author
Fricke, P., Author
Zinke, M., Author
Giller, K.1, Author              
Wall, J. S., Author
Riedel, D.2, Author              
Becker, S.1, Author              
Lange, A., Author
Affiliations:
1Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
2Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              

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Free keywords: Solid-state NMR; Alpha-synuclein; Amyloid fibril; Protofilament; STEM
 Abstract: Intra-neuronal aggregation of alpha-synuclein into fibrils is the molecular basis for alpha-synucleinopathies, such as Parkinson's disease. The atomic structure of human alpha-synuclein (hAS) fibrils was recently determined by Tuttle et al. using solid-state NMR (ssNMR). The previous study found that hAS fibrils are composed of a single protofilament. Here, we have investigated the structure of mouse alpha-synuclein (mAS) fibrils by STEM and isotope-dilution ssNMR experiments. We found that in contrast to hAS, mAS fibrils consist of two or even three protofilaments which are connected by rather weak interactions in between them. Although the number of protofilaments appears to be different between hAS and mAS, we found that they have a remarkably similar secondary structure and protofilament 3D structure as judged by secondary chemical shifts and intra-molecular distance restraints. We conclude that the two mutant sites between hAS and mAS (positions 53 and 87) in the fibril core region are crucial for determining the quaternary structure of alpha-synuclein fibrils.

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Language(s): eng - English
 Dates: 2018-04-172019-04-01
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.jsb.2018.04.003
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Title: Journal of Structural Biology
Source Genre: Journal
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Pages: - Volume / Issue: 206 (1) Sequence Number: - Start / End Page: 43 - 48 Identifier: -