Fig. 3: Secondary structural composition of the fibrils.
From: Light chain mutations contribute to defining the fibril morphology in systemic AL amyloidosis
a Location of the fibril cross-β structure in the sequence of the four fibril proteins. The numbering reflects the residue numbers of the respective precursor LCs after the removal of their signal sequences. Continuous lines refer to the ordered regions observed in the 3D map. Structurally disordered regions are shown as dotted lines. Cysteine residues participating in disulphide bonds are indicated in yellow. b Cross-sectional views of the four fibril proteins. The swirl of the amyloid key is indicated by the grey rotational arrow.
