Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils

White, H. E. and Hodgkinson, J. L. and Jahn, T. R. and Cohen-Krausz, S. and Gosal, W. S. and Müller, S. and Orlova, E. V. and Radford, S. E. and Saibil, H. R.. (2009) Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils. Journal of molecular biology, Vol. 389, H. 1. pp. 48-57.

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Official URL: http://edoc.unibas.ch/dok/A5262459

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Amyloid fibrils are ordered polymers in which constituent polypeptides adopt a non-native fold. Despite their importance in degenerative human diseases, the overall structure of amyloid fibrils remains unknown. High-resolution studies of model peptide assemblies have identified residues forming cross-beta-strands and have revealed some details of local beta-strand packing. However, little is known about the assembly contacts that define the fibril architecture. Here we present a set of three-dimensional structures of amyloid fibrils formed from full-length beta(2)-microglobulin, a 99-residue protein involved in clinical amyloidosis. Our cryo-electron microscopy maps reveal a hierarchical fibril structure built from tetrameric units of globular density, with at least three different subunit interfaces in this homopolymeric assembly. These findings suggest a more complex superstructure for amyloid than hitherto suspected and prompt a re-evaluation of the defining features of the amyloid fold.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Müller, Shirley
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:21
Deposited On:22 Mar 2012 13:24

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