Fig. 2: Cryo-EM structures of IGLV3-19-derived AL amyloid fibrils.
From: Light chain mutations contribute to defining the fibril morphology in systemic AL amyloidosis
a Side views of the molecular models of FOR103, FOR010 and FOR005 (A and B) fibrils. The FOR103 structure is right-hand twisted. The other fibrils possess a left-hand twist. b Cross-sectional views of one molecular layer of the four fibrils. The first and last residues of the ordered regions (ribbon diagrams with side chains) are highlighted. Structurally disordered regions are represented as dotted lines. The disulphide bond is shown in a space-filled representation (yellow). The N-terminal ordered region is coloured in blue in all panels, while the C-terminal region is consistently coloured orange.
