Antigen recognition by antibody C836 through adjustment of V(L)/V(H) packing

  • Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1165-7. doi: 10.1107/S1744309111027746.
Alexey Teplyakov  1 ,  Galina Obmolova ,  Thomas Malia ,  Gary Gilliland
Affiliations
  • 1. Centocor R&D Inc., 145 King of Prussia Road, Radnor, PA 19087, USA. [email protected]
PMID: 22102019 DOI: 10.1107/S1744309111027746
Abstract

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.

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