(1)H, (13)C and (15)N resonance assignment of 6aJL2(R25G), a highly fibrillogenic lambdaVI light chain variable domain.
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.
Gutiérrez-González
Luis H
LH
Departamento de Biotecnología, Universidad Autónoma Metropolitana-Iztapalapa, Mexico City, Mexico.
Muresanu
Lucia
L
del Pozo-Yauner
Luis
L
Sánchez
Rosalba
R
Guereca
Leopoldo
L
Becerril
Baltazar
B
Lücke
Christian
C
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D007135:Immunoglobulin Variable Region / Q000737:chemistry*; D007146:Immunoglobulin lambda-Chains / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons
D000682:Amyloid; D002247:Carbon Isotopes; D007135:Immunoglobulin Variable Region; D007146:Immunoglobulin lambda-Chains; D009587:Nitrogen Isotopes; D011522:Protons