Future directions

The future of structural work in the antibody-antigen complex field will probably be driven by four forces: 1) the use of antibody-antigen complexes as model systems for examining protein-protein interactions, which includes the ability of the immune system to find multiple solutions to binding to the same surface (epitope); 2) the study of camelid antibodies, which have single, heavy-chain binding domains rather than the more common V, :V,, heterodimers (an example of a camel antibody-lysozyme complex has recently been determined (Table 1)); 3) the use of antibodies to crystallize complexes of otherwise refractory proteins, such as human immunodeficiency virus (HIV) reverse transcriptase and cytochrome c oxidase (Table 1); and 4) a desire to understand the structural basis of catalytic antibodies of which four examples already exist (Table 1).

See also: Antibodies, specificity; Antibody-antigen intermolecular forces; Antigen-binding site; Diversity, generation of; Domains, immunoglobulin-type; Idiotype; Idiotype, internal image; IgA; IgE; Immunoglobulin structure; Monoclonal antibodies (mAbs).

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