The modeled structure of the IgG Gar VL region and its implications for anti-flavin and anti-DNP fine specificities.
The variable domain (V) sequence of the lambda-light chain of the Gar IgG2 human myeloma protein was determined from enzymatically generated peptides that were isolated, characterized, and ordered by overlap and/or by subgroup homology. The sequence consisted of the amino terminal 107 residues of the light chain, and shared subgroup V lambda III-specific residues as well as a pattern of CDR deletions unique to most V lambda III sequences. The structural role of the light V region in the high affinity for flavins and the low affinity for 2,4-dinitrophenyl haptens characteristic of the intact IgG molecule was coarsely assessed by way of model building and by comparison with the refined combining site model of MOPC 315, an Ig with relative affinity values for DNP and riboflavin the converse of those observed in Gar.
D000595:Amino Acid Sequence; D000818:Animals; D000915:Antibody Affinity; D003165:Complement System Proteins / Q000235:genetics; D004136:Dinitrobenzenes / Q000276:immunology / Q000378:metabolism; D005415:Flavins / Q000276:immunology / Q000378:metabolism; D006801:Humans; D007135:Immunoglobulin Variable Region; D007146:Immunoglobulin lambda-Chains / Q000302:isolation & purification; D051379:Mice; D008954:Models, Biological; D009194:Myeloma Proteins / Q000378:metabolism*; D011487:Protein Conformation
D004136:Dinitrobenzenes; D005415:Flavins; D007135:Immunoglobulin Variable Region; D007146:Immunoglobulin lambda-Chains; D009194:Myeloma Proteins; D003165:Complement System Proteins