Unknown

Dataset Information

0

AL amyloid fibril from a glycosylated lambda 1 light chain


ABSTRACT:

SUBMITTER: Marcus Fändrich 

PROVIDER: EMPIAR-10730 | biostudies-other |

REPOSITORIES: biostudies-other

altmetric image

Publications


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]