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. Author manuscript; available in PMC: 2018 Nov 27.
Published in final edited form as: FEBS J. 2017 Feb 1;284(3):429–450. doi: 10.1111/febs.13989

Figure 8.

Figure 8

A stereoview of the carbohydrate-binding sites in BfL (colored gray) and in a homologous lectin VVLB4 (green). The comparison is based on the coordinates of the complex of BfL with Tn-168 (monomer A, orthorhombic crystals) and the structure of VVLB4 with Tn-Ser ligand (PDB code 1N47, monomer A). Both pockets are superimposed based on positions of all atoms in the GalNAc residue; however, only the BfL ligand, Tn-168, is shown in this figure. The protein residues in both lectins are depicted as thick sticks. The α-D-GalNAc residue, common to all Tn antigens, is drawn in ball-and-stick representation, while the peptidic part of the ligand is shown as thin sticks. The loop contributing residues Gly212, Leu213, Asn214 in VVLB4, shown at the right hand side of the figure, is significantly shorter in BfL (not visible here).