Annual Review of Immunology Volume 25 2007 by Annual Reviews

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Deglycosylated IgE is shown for comparison (bottom right). An IgE Fab is highlighted (top right), showing Asn-140 and Asn-218 occupied by oligosaccharides in a single orientation. However, in vivo, glycans are very flexible; therefore, the sugar at Asn-168 is represented by a series of plausible conformational overlays to indicate the large surface area of the protein that can be shielded. See Figure 1 for color code. Oligomannose glycans: N-linked glycans that contain from 5–9 mannose residues attached to the chitobiose core 28 and 12% oligomannose glycans.

Chem. 277:29005–11 16. Mimura Y, Sondermann P, Ghirlando R, Lund J, Young SP, et al. 2001. Role of oligosaccharide residues of IgG1-Fc in FcγRIIb binding. J. Biol. Chem. 276:45539–47 17. Dong X, Storkus WJ, Salter RD. 1999. Binding and uptake of agalactosyl IgG by mannose receptor on macrophages and dendritic cells. J. Immunol. 163:5427–34 18. Sutton BJ, Phillips DC. 1983. The three-dimensional structure of the carbohydrate within the Fc fragment of immunoglobulin G. Biochem. Soc. Trans. 11(Pt.

Butler M, Quelhas D, Critchley AJ, Carchon H, Hebestreit HF, et al. 2003. Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis. Glycobiology 13:601–22 21. Jefferis R, Lund J, Mizutani H, Nakagawa H, Kawazoe Y, et al. 1990. A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins. Biochem. J. 268:529–37 22. Wormald MR, Rudd PM, Harvey DJ, Chang SC, Scragg IG, et al.

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