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-Structure paper
Title | Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 113, Issue 22, Page 6200-6205, Year 2016 |
Publish date | May 31, 2016 |
Authors | Andreas Schmidt / Karthikeyan Annamalai / Matthias Schmidt / Nikolaus Grigorieff / Marcus Fändrich / |
PubMed Abstract | 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 ...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 links | Proc Natl Acad Sci U S A / PubMed:27185936 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 8.3 Å |
Structure data | EMDB-3128: |
Source |
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