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

Rebecca Nelson, Michael R. Sawaya, Melinda Balbirnie, Anders Ø. Madsen, Christian Riekel, Robert Grothe and David Eisenberg ()
Additional contact information
Rebecca Nelson: UCLA
Michael R. Sawaya: UCLA
Melinda Balbirnie: UCLA
Anders Ø. Madsen: University of Copenhagen
Christian Riekel: European Synchrotron Radiation Facility
Robert Grothe: UCLA
David Eisenberg: UCLA

Nature, 2005, vol. 435, issue 7043, 773-778

Abstract: 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.

Date: 2005
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DOI: 10.1038/nature03680

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