By Frank J. Dixon (Eds.)
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The existing crystal structures appear to concur with peptide mapping data, discussed in Section IV. Crystallographically defined epitopes on proteins consist of conformationally adjacent, continuous ANTIBODY BINDING TO PROTEIN ANTIGENS 25 pieces of sequence (similar to the clusters observed from peptide mapping data on MHr discussed in Section IV). The advantage of analyzing crystallographic structures is that all residues in the interface area can be identified. , 1986), identify only some of the side chains that are critical for competitive binding or are near the center of the binding site.
8D) clearly does not match the pattern of immunological reactivity as well as the mobility and inverted packing density profiles. The highly reactive site a t hexapeptide 4 is a hydrophilicity minimum, and the highest hydrophilicity peaks a t hexapeptides 22 and 74, which correspond to valleys in the mobility and inverted packing density plots, show only average and low-reactivity values, respectively, for both titer and frequency. 4. Shape Accessibility and Exposed Surface Area Half (59) of the residues of MHr are accessible to a probe sphere of 15-A radius, and another 7 residues are accessible to spheres of 11- to 14-f%radius, suggesting that 56% of the residues are directly available to the ends of a fairly flat antibody binding region.
Thus, most evidence indicates that the lysozyme regions, bound by antibodies in the crystallographically characterized complexes, are relatively mobile. , 1987). , 1985). Therefore, the adjusted MHr temperature factors should reflect mobility accurately, allowing assessment of differential mobility in this antigen. Of course, a critical role for local mobility in functionally important, inducible complementarity would not require equal mobility of all portions of the antibody or antigen interface.