Solid-state NMR chemical shift assignments for AL-09 V_L immunoglobulin light chain fibrils.

ABSTRACT: Light chain (AL) amyloidosis is a systemic disease characterized by the formation of immunoglobulin light-chain fibrils in critical organs of the body. The light-chain protein AL-09 presents one severe case of cardiac AL amyloidosis, which contains seven mutations in the variable domain (V_L) relative to its germline counterpart, κI O18/O8 V_L. Three of these mutations are non-conservative-Y87H, N34I, and K42Q-and previous work has shown that they are responsible for significantly reducing the protein's thermodynamic stability, allowing fibril formation to occur with fast kinetics and across a wide-range of pH conditions. Currently, however, there is extremely limited structural information available which explicitly describes the residues that are involved in supportin

SUBMITTER: Piehl DW 

PROVIDER: S-EPMC5344749 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature