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


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.

SUBMITTER: Teplyakov A 

PROVIDER: S-EPMC3212354 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

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

Teplyakov Alexey A   Obmolova Galina G   Malia Thomas T   Gilliland Gary G  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110924 Pt 10


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. ...[more]

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