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On the Cover: Model of the extracellular domains of Fc&agr;RI showing IgA binding residues. The ectodomains of
the Fc&agr;R model are shown with the &agr; carbon trace as a blue ribbon. The membrane-proximal, transmembrane,
and cytoplasmic regions have not been modeled. The side chains of residues mutated in this study that are
important in IgA binding are shown as solid symbols. The residues marked on the ribbon in gray produced no
significant change in IgA binding activity when mutated to alanine. The His residues marked on the ribbon in
magenta produced no change in IgA binding activity when mutated to alanine or glutamate in our previous
study. The labeled residues colored red were essential for binding (>100-fold decrease in affinity). Orange and
yellow residues were of lesser importance in IgA binding when tested by mutation to alanine. All these residues
lie on a single face of the receoptor, with the F-G loop forming a prominent bulge. The proposed orientation
allows the binding surface to be displayed away from the cell surface. B is related to A by 90° rotation about
the y-axis. (Figure 7 from Wines, B. D., C. T. Sardjono, H. M. Trist, C. S. Lay, and P. M. Hogarth. The interaction
of Fc&agr;RI with IgA and its implications for ligand binding by immunoreceptors of the leukocyte receptor cluster.
J. Immunol.166:1781.)
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