Atomic structures of amyloid cross-β spines reveal varied steric zippers

Michael R. Sawaya, Shilpa Sambashivan, Rebecca Nelson, Magdalena I. Ivanova, Stuart A. Sievers, Marcin I. Apostol, Michael J. Thompson, Melinda Balbirnie, Jed J. W. Wiltzius, Heather T. McFarlane, Anders Ø. Madsen, Christian Riekel and David Eisenberg ()
Additional contact information
Michael R. Sawaya: Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA
Shilpa Sambashivan: Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA
Rebecca Nelson: Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA
Magdalena I. Ivanova: Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA
Stuart A. Sievers: Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA
Marcin I. Apostol: Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA
Michael J. Thompson: Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA
Melinda Balbirnie: Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA
Jed J. W. Wiltzius: Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA
Heather T. McFarlane: Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA
Anders Ø. Madsen: Centre for Crystallographic Studies, University of Copenhagen, Universitetsparken 5, DK-2100 KBH, Denmark
Christian Riekel: European Synchrotron Radiation Facility, BP 220, F-38043 Grenoble Cedex, France
David Eisenberg: Howard Hughes Medical Institute, UCLA-DOE Institute of Genomics and Proteomics, Los Angeles, California 90095-1570, USA

Nature, 2007, vol. 447, issue 7143, 453-457

Abstract: Abstract Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-β spine. The atomic architecture of a spine, from the fibril-forming segment GNNQQNY of the yeast prion protein Sup35, was recently revealed by X-ray microcrystallography. It is a pair of β-sheets, with the facing side chains of the two sheets interdigitated in a dry ‘steric zipper’. Here we report some 30 other segments from fibril-forming proteins that form amyloid-like fibrils, microcrystals, or usually both. These include segments from the Alzheimer’s amyloid-β and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, α-synuclein and β2-microglobulin, suggesting that common structural features are shared by amyloid diseases at the molecular level. Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.

Date: 2007
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DOI: 10.1038/nature05695

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