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TitleCryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 113, Issue 22, Page 6200-6205, Year 2016
Publish dateMay 31, 2016
AuthorsAndreas Schmidt / Karthikeyan Annamalai / Matthias Schmidt / Nikolaus Grigorieff / Marcus Fändrich /
PubMed AbstractAmyloid fibrils are proteinaceous aggregates associated with diseases in humans and animals. The fibrils are defined by intermolecular interactions between the fibril-forming polypeptide chains, but ...Amyloid fibrils are proteinaceous aggregates associated with diseases in humans and animals. The fibrils are defined by intermolecular interactions between the fibril-forming polypeptide chains, but it has so far remained difficult to reveal the assembly of the peptide subunits in a full-scale fibril. Using electron cryomicroscopy (cryo-EM), we present a reconstruction of a fibril formed from the pathogenic core of an amyloidogenic immunoglobulin (Ig) light chain. The fibril density shows a lattice-like assembly of face-to-face packed peptide dimers that corresponds to the structure of steric zippers in peptide crystals. Interpretation of the density map with a molecular model enabled us to identify the intermolecular interactions between the peptides and rationalize the hierarchical structure of the fibril based on simple chemical principles.
External linksProc Natl Acad Sci U S A / PubMed:27185936 / PubMed Central
MethodsEM (helical sym.)
Resolution8.3 Å
Structure data

EMDB-3128:
Structure of a cross-beta amyloid fibril from IGSNVVTWYQQL peptide of AL-DIA immunoglobulin light chain by cryo-EM and fiber diffraction
Method: EM (helical sym.) / Resolution: 8.3 Å

Source
  • Homo sapiens (human)

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