Structure
Each immunoglobulin light-chain molecule contains approximately 220 amino acids in a single polypeptide chain that is folded to form constant and variable region domains. Each domain comprises two β-pleated sheets. The sheets are linked by a disulfide bridge and together form a roughly barrel-shaped structure known as a β-barrel. The variable (V) domain of light chains has a high degree of structural diversity, particularly the antigen-binding region. In addition, the first 23 amino acids of the 1st variable domain framework region have a number of variations known as subgroups. Four kappa (Vκ1–Vκ4) and six lambda subgroups (Vλ1–Vλ6) can be identified. The specific subgroup structures influence the potential of the free light chains to polymerise such that AL amyloidosis is associated with Vλ6 and light-chain deposition disease with Vκ1 and Vκ4.
Read more about this topic: Serum Free Light Chain Measurement
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