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Comment
. 2013 Sep 17;110(38):E3544-6.
doi: 10.1073/pnas.1310657110. Epub 2013 Aug 8.

Crystal structure of sialylated IgG Fc: implications for the mechanism of intravenous immunoglobulin therapy

Max Crispin  1 , Xiaojie Yu, Thomas A Bowden
Affiliations
Comment

Crystal structure of sialylated IgG Fc: implications for the mechanism of intravenous immunoglobulin therapy

Max Crispin 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.
Crystal structure of sialylated IgG1 sFc. (A) HPLC of fluorescently-labeled N-linked glycans released from recombinant, hypersialylated IgG Fc. Hypersialylation and HPLC analysis was performed as previously described (5). (B) Overlay of sFc (gray) with the asialylated glycoforms (blue; PDB ID code 1H3Y). (C) Structure of sFc with monosaccharide residues colored according to A with close-up views of the glycans with a 2Fo−Fc electron density map contoured around the glycans at 1σ. For crystallographic analysis, sFc (6.5 mg/mL) was crystallized at 25 °C in 4.0 M NaCl, 0.1 M citrate pH 4.0 using the sitting-drop vapor-diffusion method using 100 nL protein plus 100 nL precipitant equilibrated against 95-μL reservoirs. Crystals were flash-frozen by immersion in a cryoprotectant containing the mother liquor diluted in 5 M NaCl and then rapidly transferred to a gaseous nitrogen stream. X-ray diffraction data were recorded at the Beamline I04 at Diamond Light Source, Oxfordshire, England. Data were processed and scaled using XIA2 and the structure was solved using Phaser with native Fc (PDB ID code 3AVE) as a search model. Model building was performed with Coot and iteratively refined in the CCP4 supported program REFMAC5. Coordinates and structure factors of sFc have been deposited in the Protein Data Bank (PDB ID code 4BYH).
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References

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