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• W2950883859 abstract "Systemic light chain (AL) amyloidosis is a life-threatening disease caused by aggregation and deposition of monoclonal immunoglobulin light chains (LC) in target organs. Severity of heart involvement is the most important factor determining prognosis. Here, we report the 4.0 Å resolution cryo-electron microscopy (cryo-EM) map and structural model of amyloid fibrils extracted from the heart of an AL patient affected by severe amyloid cardiomyopathy. The fibrils are composed of one asymmetric protofilament, showing typical 4.9 Å stacking and parallel cross-β architecture. Two distinct polypeptide stretches belonging to the LC variable domain (V l ) could be modelled in the density (total of 77 residues), stressing the role of the V l domain in fibril assembly and LC aggregation. Despite high levels of V l sequence variability, residues stabilising the observed fibril core are conserved through several V l domains, highlighting structural motifs that may be common to misfolded LCs. Our data shed first light on the architecture of life-threatening LC amyloid deposits, and provide a rationale for correlating LC amino acid sequences and fibril structures." @default.
• W2950883859 created "2019-06-27" @default.
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• W2950883859 date "2018-10-16" @default.
• W2950883859 modified "2023-09-27" @default.
• W2950883859 title "Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain (AL) amyloidosis patient" @default.
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• W2950883859 doi "https://doi.org/10.1101/444901" @default.
• W2950883859 hasPublicationYear "2018" @default.
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