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Comment
. 2008 Mar 18;105(11):4081-2.
doi: 10.1073/pnas.0801192105. Epub 2008 Mar 14.

Making autoantibodies safe

Christopher N Scanlan  1 , Dennis R Burton, Raymond A Dwek
Affiliations
Comment

Making autoantibodies safe

Christopher N Scanlan et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
The two conserved N-linked carbohydrate chains of IgG are attached to Asn-297 of the Cγ2 domains of each IgG heavy chain. A sialylated biantennary glycan is shown [based on published crystallographic data (3, 15), with nonreducing sialic acid residues modeled according to likely linkage constraints]. The close packing of the carbohydrates between the two chains is evident. A range of other glycoforms also exists on serum IgG (13). These other glycans are based mostly on the biantennary structure but without some or all of the sialic acid or galactose residues from the nonreducing terminus (or fucose residues from the core). The presence of a particular carbohydrate maintains a defined structure of the Fc region, with specific consequences for Fc effector function. Some of the key glycan-mediated interactions are indicated.
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