Sie befinden Sich nicht im Netzwerk der Universität Paderborn. Der Zugriff auf elektronische Ressourcen ist gegebenenfalls nur via VPN oder Shibboleth (DFN-AAI) möglich. mehr Informationen...
Globular Tetramers of beta sub(2)-Microglobulin Assemble into Elaborate Amyloid Fibrils
Ist Teil von
Journal of molecular biology, 2009-05, Vol.389 (1), p.48-57
Erscheinungsjahr
2009
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
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 sub(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.
Sprache
Englisch
Identifikatoren
ISSN: 0022-2836
eISSN: 1089-8638
DOI: 10.1016/j.jmb.2009.03.066
Titel-ID: cdi_proquest_miscellaneous_20574559
Format
–
Weiterführende Literatur
Empfehlungen zum selben Thema automatisch vorgeschlagen von bX