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TitleCryo-EM structure of alpha-synuclein fibrils.
Journal, issue, pagesElife, Vol. 7, Year 2018
Publish dateJul 3, 2018
AuthorsRicardo Guerrero-Ferreira / Nicholas Mi Taylor / Daniel Mona / Philippe Ringler / Matthias E Lauer / Roland Riek / Markus Britschgi / Henning Stahlberg /
PubMed AbstractParkinson'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 ...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.
External linksElife / PubMed:29969391 / PubMed Central
MethodsEM (helical sym.)
Resolution3.4 Å
Structure data

0148

6h6b

EMDB-0148, PDB-6h6b:
Structure of alpha-synuclein fibrils
Method: EM (helical sym.) / Resolution: 3.4 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Parkinson's disease / apha-synuclein / fibril / filament

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