Roles for glycosylation in the anti-inflammatory molecule CD59
Rudd PM, Morgan BP, Wormald MR, Harvey DJ, van den Berg CW, Davis SJ, Ferguson MA, Dwek RA. (1997), Biochem Soc Trans. 25, 1177-84
Key figure: Comparison of the normal-phase HPLC profiles of 2-aminobenzamide-labelled glycans released from CD59 isolated from HuE
The elution positions of the dextran ladder and of the different classes of oligosaccharides are shown in the scale above and the bars overlaid on the Figure. The insert shows a molecular model of CD59 based on the protein co-ordinates from the solution structure . The binding-site residues (modelled with van der Waals surfaces in white close-packed notation) are located at Trp-40, Asp-24, Arg-53 and Glu-56 . The glycan anchor is modelled with a tri-mannosyl core, an ethanolamine bridge at Man3 and additional ethanolamine groups at Man1 and Man2. Two lipids are attached to inositol via a phosphate and the third is attached directly to the inositol ring through an ester linkage. A trisialylated, tetra-antennary complex N-glycan is shown attached to Asn-18. The O-glycan, NeuNAc2,3Galβ1-3GalNAc, is attached to Thr-51 to indicate one of the possible linkage positions. Thr and Ser hydroxyl side chains in the protein are numbered. The sugar chains and the glycan contained within the GPI anchor are depicted in black ‘ball and stick’ notation. G, Gal; F, Fuc.