Cryo-EM structure of alpha-synuclein fibrils

Guerrero-Ferreira, Ricardo and Taylor, Nicholas M. I. and Mona, Daniel and Ringler, Philippe and Lauer, Matthias E. and Riek, Roland and Britschgi, Markus and Stahlberg, Henning. (2018) Cryo-EM structure of alpha-synuclein fibrils. eLife, 7. e36402.

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Official URL: https://edoc.unibas.ch/64950/

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Parkinson's disease is a progressive neuropathological disorder that belongs to the class of synucleopathies, in which the protein alpha-synuclein is found at abnormally high concentrations in affected neurons. Its hallmark are intracellular inclusions called Lewy bodies and Lewy neurites. We here report the structure of cytotoxic alpha-synuclein fibrils (residues 1-121), determined by cryo-electron microscopy structure at a resolution of 3.4Å. Two protofilaments form a polar fibril composed of staggered β-strands. The backbone of residues 38 to 95, including the fibril core and the non-amyloid component region, are well resolved in the EM map. Residues 50-57, containing three of the mutation sites associated with familial synucleinopathies, form the interface between the two protofilaments and contribute to fibril stability. A hydrophobic cleft at one end of the fibril may have implications for fibril elongation, and invites for the design of molecules for diagnosis and treatment of synucleinopathies.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Stahlberg)
UniBasel Contributors:Stahlberg, Henning
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:27 Apr 2020 10:02
Deposited On:27 Apr 2020 10:02

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