The Critical Role of the Variable Domain in Driving Proteotoxicity and Aggregation in Full-length Light Chains

Abstract excerpt

• CL domain stabilizes the VL domain and full-length AL55. • The crystal structure of AL55 reveals a non-canonical open conformation. • Non-native interactions between VL domains of adjacent dimers are formed in the crystals. • Full-length AL55 dimers are the most cardiotoxic species. • In vitro aggregation of VL domains does not recapitulate in vivo fibril morphology. Light chain (AL) amyloidosis is the most...

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