Fig. 3 | Nature Communications

Fig. 3

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

Fig. 3

Location of specific sequence elements in the structure. a Hydrophobicity (gray) and aggregation score (brown) of the ordered part of the fibril protein. Magenta letters: mutations compared to the IGLV1-44 germ line segment. Boxes: CDRs. Residue numbers refer to the native LC without signal sequence. b Fibril protein showing the residue-specific aggregation score (0–5). c Electrostatic surface representation of the fibril protein. d Fibril protein with CDRs (black) and mutations (magenta) highlighted. e Ribbon diagram of a native VL domain (PDB entry 1BJM)60 showing residues 3–113. CDRs are colored black; mutations are colored in red if they affect the core (residue 76), purple (surface residues with potential relevance for domain–domain interactions), or magenta (other surface residues)

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