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Structure of the cross-β spine of amyloid-like fibrils

Author

Listed:
  • Rebecca Nelson

    (UCLA)

  • Michael R. Sawaya

    (UCLA)

  • Melinda Balbirnie

    (UCLA)

  • Anders Ø. Madsen

    (University of Copenhagen
    European Synchrotron Radiation Facility)

  • Christian Riekel

    (European Synchrotron Radiation Facility)

  • Robert Grothe

    (UCLA)

  • David Eisenberg

    (UCLA)

Abstract

Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and amyloid-like fibrils can be formed in vitro. For the yeast protein Sup35, conversion to amyloid-like fibrils is associated with a transmissible infection akin to that caused by mammalian prions. A seven-residue peptide segment from Sup35 forms amyloid-like fibrils and closely related microcrystals, from which we have determined the atomic structure of the cross-β spine. It is a double β-sheet, with each sheet formed from parallel segments stacked in register. Side chains protruding from the two sheets form a dry, tightly self-complementing steric zipper, bonding the sheets. Within each sheet, every segment is bound to its two neighbouring segments through stacks of both backbone and side-chain hydrogen bonds. The structure illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures.

Suggested Citation

  • Rebecca Nelson & Michael R. Sawaya & Melinda Balbirnie & Anders Ø. Madsen & Christian Riekel & Robert Grothe & David Eisenberg, 2005. "Structure of the cross-β spine of amyloid-like fibrils," Nature, Nature, vol. 435(7043), pages 773-778, June.
    • Handle: RePEc:nat:nature:v:435:y:2005:i:7043:d:10.1038_nature03680
    DOI: 10.1038/nature03680
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    Cited by:

    1. Massih Khorvash & Nick Blinov & Carol Ladner-Keay & Jie Lu & Judith M Silverman & Ebrima Gibbs & Yu Tian Wang & Andriy Kovalenko & David Wishart & Neil R Cashman, 2020. "Molecular interactions between monoclonal oligomer-specific antibody 5E3 and its amyloid beta cognates," PLOS ONE, Public Library of Science, vol. 15(5), pages 1-35, May.
    2. Deena M A Gendoo & Paul M Harrison, 2011. "Origins and Evolution of the HET-s Prion-Forming Protein: Searching for Other Amyloid-Forming Solenoids," PLOS ONE, Public Library of Science, vol. 6(11), pages 1-12, November.
    3. Vishruth Mullapudi & Jaime Vaquer-Alicea & Vaibhav Bommareddy & Anthony R. Vega & Bryan D. Ryder & Charles L. White & Marc. I. Diamond & Lukasz A. Joachimiak, 2023. "Network of hotspot interactions cluster tau amyloid folds," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    4. Allen W Bryan Jr. & Matthew Menke & Lenore J Cowen & Susan L Lindquist & Bonnie Berger, 2009. "BETASCAN: Probable β-amyloids Identified by Pairwise Probabilistic Analysis," PLOS Computational Biology, Public Library of Science, vol. 5(3), pages 1-11, March.
    5. Kübra Kaygisiz & Lena Rauch-Wirth & Arghya Dutta & Xiaoqing Yu & Yuki Nagata & Tristan Bereau & Jan Münch & Christopher V. Synatschke & Tanja Weil, 2023. "Data-mining unveils structure–property–activity correlation of viral infectivity enhancing self-assembling peptides," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    6. Thomas Heerde & Desiree Schütz & Yu-Jie Lin & Jan Münch & Matthias Schmidt & Marcus Fändrich, 2023. "Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril," Nature Communications, Nature, vol. 14(1), pages 1-8, December.
    7. Victor Banerjee & Rajiv K Kar & Aritreyee Datta & Krupakar Parthasarathi & Subhrangsu Chatterjee & Kali P Das & Anirban Bhunia, 2013. "Use of a Small Peptide Fragment as an Inhibitor of Insulin Fibrillation Process: A Study by High and Low Resolution Spectroscopy," PLOS ONE, Public Library of Science, vol. 8(8), pages 1-15, August.
    8. Sanne Abeln & Michele Vendruscolo & Christopher M Dobson & Daan Frenkel, 2014. "A Simple Lattice Model That Captures Protein Folding, Aggregation and Amyloid Formation," PLOS ONE, Public Library of Science, vol. 9(1), pages 1-8, January.
    9. Andrew C Gill, 2014. "β-Hairpin-Mediated Formation of Structurally Distinct Multimers of Neurotoxic Prion Peptides," PLOS ONE, Public Library of Science, vol. 9(1), pages 1-17, January.

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