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TitleGlobular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils.
Journal, issue, pagesJ Mol Biol, Vol. 389, Issue 1, Page 48-57, Year 2009
Publish dateMay 29, 2009
AuthorsHelen E White / Julie L Hodgkinson / Thomas R Jahn / Sara Cohen-Krausz / Walraj S Gosal / Shirley Müller / Elena V Orlova / Sheena E Radford / Helen R Saibil /
PubMed AbstractAmyloid 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 ...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.
External linksJ Mol Biol / PubMed:19345691 / PubMed Central
MethodsEM (helical sym.)
Resolution25.0 - 29.0 Å
Structure data

EMDB-1613:
Globular tetramers of beta-2-microglobulin assemble into elaborate amyloid fibrils
Method: EM (helical sym.) / Resolution: 29.0 Å

EMDB-1614:
Globular tetramers of beta-2-microglobulin assemble into elaborate amyloid fibrils
Method: EM (helical sym.) / Resolution: 25.0 Å

Source
  • Homo sapiens (human)

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