Open AccessAntigen recognition by antibody C836 through adjustment of V L /V H packing
Author(s) -
Teplyakov Alexey,
Obmolova Galina,
Malia Thomas,
Gilliland Gary
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111027746
Subject(s) - monoclonal antibody , antibody , antigen , chemistry , crystallography , immunoglobulin fab fragments , rotation (mathematics) , microbiology and biotechnology , biology , immunology , geometry , mathematics , complementarity determining region
C836 is a neutralizing monoclonal antibody to human interleukin IL‐13 generated by mouse immunization. The crystal structure of the C836 Fab was determined at 2.5 Å resolution and compared with the IL‐13‐bound form determined previously. This comparison indicates an induced‐fit mechanism of antigen recognition through rigid‐body rotation of the V L and V H domains. The magnitude of this rearrangement is one of the largest observed for antibody–protein interactions.