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Soluble β‐galactosyl‐binding lectin (galectin) from toad ovary: Crystallographic studies of two protein‐sugar complexes

Galectin‐1, S‐type β‐galactosyl‐binding lectins present in vertebrate and invertebrate species, are dimeric proteins that participate in cellular adhesion, activation, growth regulation, and apoptosis. Two high‐resolution crystal structures of B. arenarum galectin‐1 in complex with two related carbohydrates, LacNAc and TDG, show that the topologically equivalent hydroxyl groups in the two disaccharides exhibit identical patterns of interaction with the protein. Groups that are not equivalent between the two sugars present in the second moiety of the disaccharide, interact differently with the protein, but use the same number and quality of interactions.