Cryo-EM structure of alpha-synuclein fibrils

Research output: Contribution to journal › Journal article › Research › peer-review

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Cryo-EM structure of alpha-synuclein fibrils. / Guerrero-Ferreira, Ricardo; Taylor, Nicholas M I; Mona, Daniel; Ringler, Philippe; Lauer, Matthias E; Riek, Roland; Britschgi, Markus; Stahlberg, Henning.

In: eLife, Vol. 7, 2018.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Guerrero-Ferreira, R, Taylor, NMI, Mona, D, Ringler, P, Lauer, ME, Riek, R, Britschgi, M & Stahlberg, H 2018, 'Cryo-EM structure of alpha-synuclein fibrils', eLife, vol. 7. https://doi.org/10.7554/eLife.36402

APA

Guerrero-Ferreira, R., Taylor, N. M. I., Mona, D., Ringler, P., Lauer, M. E., Riek, R., Britschgi, M., & Stahlberg, H. (2018). Cryo-EM structure of alpha-synuclein fibrils. eLife, 7. https://doi.org/10.7554/eLife.36402

Vancouver

Guerrero-Ferreira R, Taylor NMI, Mona D, Ringler P, Lauer ME, Riek R et al. Cryo-EM structure of alpha-synuclein fibrils. eLife. 2018;7. https://doi.org/10.7554/eLife.36402

Author

Guerrero-Ferreira, Ricardo ; Taylor, Nicholas M I ; Mona, Daniel ; Ringler, Philippe ; Lauer, Matthias E ; Riek, Roland ; Britschgi, Markus ; Stahlberg, Henning. / Cryo-EM structure of alpha-synuclein fibrils. In: eLife. 2018 ; Vol. 7.

Bibtex

@article{1ad475009cd540b6b24fd8af76353703,
title = "Cryo-EM structure of alpha-synuclein fibrils",
abstract = "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 3.4{\AA}. 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.",
author = "Ricardo Guerrero-Ferreira and Taylor, {Nicholas M I} and Daniel Mona and Philippe Ringler and Lauer, {Matthias E} and Roland Riek and Markus Britschgi and Henning Stahlberg",
note = "Nicholas M.I.Taylor : Present address: 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 ",
year = "2018",
doi = "10.7554/eLife.36402",
language = "English",
volume = "7",
journal = "eLife",
issn = "2050-084X",
publisher = "eLife Sciences Publications Ltd.",

}

RIS

TY - JOUR

T1 - Cryo-EM structure of alpha-synuclein fibrils

AU - Guerrero-Ferreira, Ricardo

AU - Taylor, Nicholas M I

AU - Mona, Daniel

AU - Ringler, Philippe

AU - Lauer, Matthias E

AU - Riek, Roland

AU - Britschgi, Markus

AU - Stahlberg, Henning

N1 - Nicholas M.I.Taylor : Present address: 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

PY - 2018

Y1 - 2018

N2 - 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.

AB - 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.

U2 - 10.7554/eLife.36402

DO - 10.7554/eLife.36402

M3 - Journal article

C2 - 29969391

VL - 7

JO - eLife

JF - eLife

SN - 2050-084X

ER -

ID: 199380706