Biomolecular NMR Assignments

, Volume 3, Issue 2, pp 255–259

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

  • Sujoy Mukherjee
  • Simon P. Pondaven
  • Nicole Höfer
  • Christopher P. Jaroniec
Article

DOI: 10.1007/s12104-009-9188-y

Cite this article as:
Mukherjee, S., Pondaven, S.P., Höfer, N. et al. Biomol NMR Assign (2009) 3: 255. doi:10.1007/s12104-009-9188-y

Abstract

1H, 13C and 15N resonance assignments are presented for a recombinant 114 amino acid human immunoglobulin (Ig) κIV light-chain variable domain (VL) LEN, which displays a high degree of sequence identity with another human Ig κIV 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 15N 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 β-sheet content. These findings are consistent with previously published biophysical data and the high-resolution X-ray structure of LEN.

Keywords

Immunoglobulin light-chainBence Jones proteinLight-chain amyloidosisProtein misfoldingNMR spectroscopy

Copyright information

© Springer Science+Business Media B.V. 2009

Authors and Affiliations

  • Sujoy Mukherjee
    • 1
  • Simon P. Pondaven
    • 1
  • Nicole Höfer
    • 1
    • 2
  • Christopher P. Jaroniec
    • 1
  1. 1.Department of ChemistryThe Ohio State UniversityColumbusUSA
  2. 2.Department of Chemical and Environmental SciencesUniversity of LimerickLimerickIreland