| Abstract: | The construction of molecular models for the human serotransferrin glycans shows that they present one compact section linked to the protein and constituted by the pentasaccharide alpha-Man-(1 leads to 3)-[alpha-Man-(1 leads to 6)]-beta-Man-(1 leads to 4)-beta-GlcNAc-(1 leads to 4)-beta-GlcNAc-(1 leads to)-Asn to which are attached two "antennae" consisting of the trisaccharide alpha-NANA-(2 leads to 6)-beta-Gal-(1 leads to 4)-beta-GlcNAc. The trisaccharide sequence beta-Man-(1 leads to 4)-beta-GlcNAc-(1 leads to 4)-beta-GlcNAc adopts a flat and rigid conformation, stabilised by hydrogen bonds. In contrast, the sequence alpha-NANA-(1 leads to 6)-beta-Gal-(1 leads to 4)-beta-GlcNAc-(1 leads to 2)-alpha-Man takes up a helical configuration. The two "antennae" can be disposed on the pentasaccharide core to give two possible configurations, one Y-shaped and the other T-shaped. In both cases, the general conformation of the glycans is perfectly compatible with their postulated role as a recognition signal. |
