By Frank J. Dixon (Eds.)
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1984). , all (approximately 7) antigen residues apparently critical to antibody binding, as indicated by various experimental techniques. Epitopes, as defined in this article, usually represent epicenters for the antibody-antigen interaction and not the total interface. Besides being compatible with most experimental methods of identifying epitopes (except X-ray crystallography 26 ELIZABETH D. GETZOFF ET A L . and some footprinting techniques, which define epitopes by their boundaries), this definition explains many apparent observations of autoimmunity provoked by molecular mimicry (Oldstone, 1987).
42 ELIZABETH D. GETZOFF ET AL. superassemblies are constructed from a connected set of microassemblies, which themselves cluster in three dimensions. These antigenic microassemblies are not restricted to clusters formed by sequencelocal neighbors. Critical residues interacting spatially within one epitope often adjoin critical residues of nearby epitopes, and together form a network of closely interacting side chains that represent the backbone of the three-dimensional superassemblies formed by the most reactive sites.
In the folded protein, the side-chain surface exposure can also be measured as a percentage of the total surface exposure of the same sidechain conformation in the absence of the other protein residues. 9. Superassemblies of MHr sequential epitopes. Three categories of immunological reactivity (red, most reactive; yellow, average; blue, least reactive) are mapped by color coding onto the solvent-exposed molecular surface of MHr, shown i n front and back views. Raster color graphics images of opposing sides of the solid external molecular surface of MHr show t h a t the most highly reactive surface regions form superassemblies (three-dimensional clusters) that wrap around one side (left view) of the protein and almost connect on the other side (right view).
Advances in Immunology by Frank J. Dixon (Eds.)