The modeled structure of the IgG Gar VL region and its implications for anti-flavin and anti-DNP fine specificities
Kiefer, C.R.; McGuire, B.S.; Osserman, E.F.; Garver, F.A.
Journal of Immunology 131(4): 1871-1875
1983
ISSN/ISBN: 0022-1767 PMID: 6413582 Document Number: 211990
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.