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Article

Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis.

Nature communications - 8 Feb 2021

Radamaker Lynn, Baur Julian, Huhn Stefanie, Haupt Christian, Hegenbart Ute, Schönland Stefan, Bansal Akanksha, Schmidt Matthias, Fändrich Marcus

Abstract excerpt

Systemic AL amyloidosis is a debilitating and potentially fatal disease that arises from the misfolding and fibrillation of immunoglobulin light chains (LCs). The disease is patient-specific with essentially each patient possessing a unique LC sequence. In this study, we present two ex vivo fibril structures of a λ3 LC. The fibrils were extracted from the explanted heart of a patient (FOR005) and consist of...

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Share to Amino Acid Sequence
Share to Amyloid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cryoelectron Microscopy

Share to Immunoglobulin Light Chains

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Source

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Identifiers

PMID: 33558536
DOI: 10.1038/s41467-021-21126-2
PMCID: PMC7870857

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