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

Acta Crystallogr Sect F Struct Biol Cryst Commun

Centocor R&D Inc., 145 King of Prussia Road, Radnor, PA 19087, USA.

Published: October 2011

AI Article Synopsis

  • C836 is a monoclonal antibody that specifically targets human interleukin IL-13, developed through mouse immunization.
  • The crystal structure of C836 Fab was resolved at 2.5 Å resolution and was analyzed alongside a previously determined IL-13-bound structure.
  • The comparison reveals a significant "induced-fit" mechanism, marked by a large rigid-body rotation of its variable domains during the binding process.

Article 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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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3212354PMC
http://dx.doi.org/10.1107/S1744309111027746DOI Listing

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