title: 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.
authors.affiliation: Centocor R&D Inc., 145 King of Prussia Road, Radnor, PA 19087, USA. ateplyak@its.jnj.com
authors.forename: Alexey
authors.initials: A
authors.lastname: Teplyakov
authors.forename: Galina
authors.initials: G
authors.lastname: Obmolova
authors.forename: Thomas
authors.initials: T
authors.lastname: Malia
authors.forename: Gary
authors.initials: G
authors.lastname: Gilliland
mesh_terms: D000818:Animals; D000941:Antigens / Q000737:chemistry* / Q000276:immunology; D018360:Crystallography, X-Ray; D007135:Immunoglobulin Variable Region / Q000737:chemistry* / Q000276:immunology; D051379:Mice; D008958:Models, Molecular; D017434:Protein Structure, Tertiary
chemical_list: D000941:Antigens; D007135:Immunoglobulin Variable Region
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