Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis

Lynn Radamaker; Yin-Hsi Lin; Karthikeyan Annamalai; Stefanie Huhn; Ute Hegenbart; Stefan O. Schönland; Günter Fritz; Matthias Schmidt; Marcus Fändrich

doi:10.1038/s41467-019-09032-0

Nature Communications (Mar 2019)

Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis

Lynn Radamaker,
Yin-Hsi Lin,
Karthikeyan Annamalai,
Stefanie Huhn,
Ute Hegenbart,
Stefan O. Schönland,
Günter Fritz,
Matthias Schmidt,
Marcus Fändrich

Affiliations

Lynn Radamaker: Institute of Protein Biochemistry, Ulm University
Yin-Hsi Lin: Institute of Protein Biochemistry, Ulm University
Karthikeyan Annamalai: Institute of Protein Biochemistry, Ulm University
Stefanie Huhn: Medical Department V, Section of Multiple Myeloma, Heidelberg University Hospital
Ute Hegenbart: Medical Department V, Amyloidosis Center, Heidelberg University Hospital
Stefan O. Schönland: Medical Department V, Amyloidosis Center, Heidelberg University Hospital
Günter Fritz: Institute of Microbiology, University of Hohenheim
Matthias Schmidt: Institute of Protein Biochemistry, Ulm University
Marcus Fändrich: Institute of Protein Biochemistry, Ulm University

DOI: https://doi.org/10.1038/s41467-019-09032-0
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 8

Abstract

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Systemic AL amyloidosis is caused by misfolding of immunoglobulin light chains and is one of the most frequently occurring forms of systemic amyloidosis. Here the authors present the 3.3 Å cryo-EM structure of a λ1 AL amyloid fibril that was isolated from an explanted human heart.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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