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© Research
Publication : The EMBO journal

Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The EMBO journal - 15 Feb 1999

Jiménez JL, Guijarro JI, Orlova E, Zurdo J, Dobson CM, Sunde M, Saibil HR

Link to Pubmed [PMID] – 10022824

EMBO J. 1999 Feb;18(4):815-21

Amyloid fibrils are assemblies of misfolded proteins and are associated with pathological conditions such as Alzheimer’s disease and the spongiform encephalopathies. In the amyloid diseases, a diverse group of normally soluble proteins self-assemble to form insoluble fibrils. X-ray fibre diffraction studies have shown that the protofilament cores of fibrils formed from the various proteins all contain a cross-beta-scaffold, with beta-strands perpendicular and beta-sheets parallel to the fibre axis. We have determined the threedimensional structure of an amyloid fibril, formed by the SH3 domain of phosphatidylinositol-3′-kinase, using cryo-electron microscopy and image processing at 25 A resolution. The structure is a double helix of two protofilament pairs wound around a hollow core, with a helical crossover repeat of approximately 600 A and an axial subunit repeat of approximately 27 A. The native SH3 domain is too compact to fit into the fibril density, and must unfold to adopt a longer, thinner shape in the amyloid form. The 20×40-A protofilaments can only accommodate one pair of flat beta-sheets stacked against each other, with very little inter-strand twist. We propose a model for the polypeptide packing as a basis for understanding the structure of amyloid fibrils in general.

http://www.ncbi.nlm.nih.gov/pubmed/10022824