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By Frank J. Dixon (Eds.)

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1972). The MHr protein fold consists of an antiparallel bundle of four a-helices (named A, B, C, and D in sequence order) that surround a two-iron center a t the active site, an N-terminal loop region, and shorter loops between the helices and a t the Cterminus. , 1987a). , 1985). , 1985a). Examination of the exposed MHr molecular surface and corrected average main-chain temperature factors by residue indicates that a large portion (over 80%) of the molecular surface is relatively mobile. , 1984).

6. Secondary Structure Although secondary structure is not a dominant factor in the degree of antigenicity, the least reactive residues in MHr are predominantly found in a-helices. Twenty-seven least reactive residues are distributed among the four helices, whereas the remaining four residues occur in the N- or C-terminal loops. 6-residue helical repeat (visible in most of the structural plots) may reduce the ability of a hexapeptide to mimic a surface region or conformational determinant of a protein antigen.

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).

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