(1)H, (13)C and (15)N resonance assignment of 6aJL2(R25G), a highly fibrillogenic lambdaVI light chain variable domain

Biomol NMR Assign. 2007 Dec;1(2):159-61. doi: 10.1007/s12104-007-9045-9. Epub 2007 Aug 22.

Abstract

An allotypic variation at position 25 influences the fibrillogenicity of lambdaVI light chains, which are related to humoral immune response and have been associated with AL amyloidosis. The full resonance assignment and a preliminary structural characterization of 6aJL2(R25G) are reported.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amyloid / chemistry*
  • Carbon Isotopes / chemistry
  • Immunoglobulin Variable Region / chemistry*
  • Immunoglobulin lambda-Chains / chemistry*
  • Magnetic Resonance Spectroscopy / methods*
  • Molecular Weight
  • Nitrogen Isotopes / chemistry
  • Protein Structure, Tertiary
  • Protons

Substances

  • Amyloid
  • Carbon Isotopes
  • Immunoglobulin Variable Region
  • Immunoglobulin lambda-Chains
  • Nitrogen Isotopes
  • Protons