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Cryo-EM structure of alpha-synuclein fibrils

Guerrero-Ferreira, Ricardo ; Taylor, Nicholas Mi ; Mona, Daniel ; Ringler, Philippe ; Lauer, Matthias E ; Riek, Roland ; Britschgi, Markus ; Stahlberg, Henning

eLife, 2018-07, Vol.7 [Periódico revisado por pares]

England: eLife Science Publications, Ltd

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Título:
Cryo-EM structure of alpha-synuclein fibrils
Autor: Guerrero-Ferreira, Ricardo ; Taylor, Nicholas Mi ; Mona, Daniel ; Ringler, Philippe ; Lauer, Matthias E ; Riek, Roland ; Britschgi, Markus ; Stahlberg, Henning
Assuntos: alpha-synuclein ; alpha-Synuclein - chemistry ; alpha-Synuclein - ultrastructure ; Amino Acid Sequence ; Brain ; Brain damage ; cryo-electron microscopy ; Cryoelectron Microscopy ; Disease transmission ; Diseases ; Displays (Marketing) ; Electron microscopy ; fibril ; Humans ; Hydrophobic and Hydrophilic Interactions ; Medical imaging equipment ; Microscopy ; Models, Molecular ; Mutation - genetics ; neurodegeneration ; Neurons ; Neuroscience ; Parkinson Disease - genetics ; Parkinson's disease ; Physicists ; Proteins ; structural biology ; Structural Biology and Molecular Biophysics ; Structure (Literature)
É parte de: eLife, 2018-07, Vol.7
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Structural Biology of Molecular Machines Group, Protein Structure and Function Programme, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Descrição: Parkinson's disease is a progressive neuropathological disorder that belongs to the class of synucleinopathies, 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 at a resolution of 3.4 Å. 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.
Editor: England: eLife Science Publications, Ltd
Idioma: Inglês

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Cryo-EM structure of alpha-synuclein fibrils

Guerrero-Ferreira, Ricardo ; Taylor, Nicholas Mi ; Mona, Daniel ; Ringler, Philippe ; Lauer, Matthias E ; Riek, Roland ; Britschgi, Markus ; Stahlberg, Henning

England: eLife Science Publications, Ltd

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