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-Structure paper
タイトル | Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 113, Issue 22, Page 6200-6205, Year 2016 |
掲載日 | 2016年5月31日 |
![]() | Andreas Schmidt / Karthikeyan Annamalai / Matthias Schmidt / Nikolaus Grigorieff / Marcus Fändrich / ![]() ![]() |
PubMed 要旨 | 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. |
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手法 | EM (らせん対称) |
解像度 | 8.3 Å |
構造データ | ![]() EMDB-3128: |
由来 |
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