Antibodyantigen Complexes Threedimensional Structures

Steven Sheriff, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey, USA

Copyright © 1998 Elsevier Ltd. All Rights Reserved.

The advent of monoclonal antibody technology has made possible structural studies of antibody-antigen complexes by providing large quantities of unique molecular entities. Since the mid-1980s, structural studies of antibody-antigen complexes have encompassed a wide variety of antigens ranging from small molecules through peptides and oligosaccharides to proteins, including several anti-idiotype-idiotype complexes (Table 1). All antibody-antigen complexes have shown that the antibody has achieved specificity and affinity through interactions of an antigen-binding site, made up principally, but not exclusively, of residues from the complementarity-determining regions (CDRs), with the antigen. However, the shape of the antigen-binding site and specific interactions have varied considerably depending on the size, shape and surface polarity of the antigen.

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