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Antibody domain mutants demonstrate autonomy of the antigen binding site.
Author(s) -
Simon T.,
Rajewsky K.
Publication year - 1990
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1990.tb08209.x
Subject(s) - cooperativity , context (archaeology) , immunoglobulin light chain , biology , microbiology and biotechnology , antibody , lambda , antigen , stereochemistry , genetics , physics , chemistry , paleontology , optics
We have constructed derivatives of a lambda I light chain‐bearing anti‐(4‐hydroxy,3‐nitrophenyl)acetyl (NP) antibody which have the V regions exchanged between heavy chains and light chains of the kappa or lambda I type. These antibodies are assembled and secreted normally, and bind haptenic and macromolecular ligands like the wild‐type; similar results are obtained for monovalent heterodimers of VHCL and lambda I light chains. The observed independence of the binding site from the constant region context argues against a role of longitudinal interactions between constant and variable domains in antigen recognition, and therefore against cooperativity between binding sites.