Crystal structure of 6aJL2-R24G light chain variable domain: Does crystal packing explain amyloid fibril formation?

ABSTRACT: Light chain amyloidosis is one of the most common systemic amyloidosis, characterized by the deposition of immunoglobulin light variable domain as insoluble amyloid fibrils in vital organs, leading to the death of patients. Germline λ6a is closely related with this disease and has been reported that 25% of proteins encoded by this germline have a change at position 24 where an Arg is replaced by a Gly (R24G). This germline variant reduces protein stability and increases the propensity to form amyloid fibrils. In this work, the crystal structure of 6aJL2-R24G has been determined to 2.0 Å resolution by molecular replacement. Crystal belongs to space group I2₁2₁2₁ (PDB ID 5JPJ) and there are two molecules in the asymmetric unit. This 6aJL2-R24G structure as se

SUBMITTER: Rudino-Pinera E 

PROVIDER: S-EPMC6728755 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature