Backbone and side-chain (1)H, (13)C and (15)N resonance assignments of LEN, a human immunoglobulin kappaIV light-chain variable domain

(1)H, (13)C and (15)N resonance assignments are presented for a recombinant 114 amino acid human immunoglobulin (Ig) kappaIV light-chain variable domain (VL) LEN, which displays a high degree of sequence identity with another human Ig kappaIV VL, SMA. While SMA is highly amyloidogenic in vivo and in vitro and has been linked to the pathogenesis of light-chain amyloidosis, LEN is non-amyloidogenic in vivo and can be converted to the amyloid state only in vitro under destabilizing conditions. Measurements of longitudinal and transverse amide (15)N relaxation rates confirm that, as expected, LEN is a dimer at physiological pH and typical concentrations used for NMR studies, and the analysis of secondary chemical shifts indicates that the protein has a high beta-sheet content. These findings are consistent with previously published biophysical data and the high-resolution X-ray structure of LEN.