Dataset Information
AL amyloid fibril from a glycosylated lambda 1 light chain
Ontology highlight
ABSTRACT:
SUBMITTER: Marcus Fändrich
PROVIDER: EMPIAR-10730 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM.
Nature communications 20211105 1
Systemic AL amyloidosis is a rare disease that is caused by the misfolding of immunoglobulin light chains (LCs). Potential drivers of amyloid formation in this disease are post-translational modifications (PTMs) and the mutational changes that are inserted into the LCs by somatic hypermutation. Here we present the cryo electron microscopy (cryo-EM) structure of an ex vivo λ1-AL amyloid fibril whose deposits disrupt the ordered cardiomyocyte structure in the heart. The fibril protein contains six ...[more]
