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

Mario A. Bianchet, Hafiz Ahmed, Gerardo R. Vasta, L. Mario Amzel

Research output: Contribution to journalArticlepeer-review

68 Scopus citations


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. The structures show additional protein-carbohydrate interactions not present in previously reported lectin-lactose complexes. These contacts provide an explanation for the enhanced affinity of galectin-1 for TDG and LacNAc relative to lactose. Galectins are in dimer-monomer equilibrium at physiological protein concentrations, suggesting that this equilibrium may be involved in organ-specific regulation of activity. Comparison of B. arenarum with other galectin-1 structures shows that among different galectins there are significant changes in accessible surface area buried upon dimer formation, providing a rationale for the variations observed in the free-energies of dimerization. The structure of the B. arenarum galectin-1 has a large cleft with a strong negative potential that connects the two binding sites at the surface of the protein. Such a striking characteristic suggests that this cleft is probably involved in interactions of the galectin with other intra or extra-cellular proteins. (C) 2000 Wiley-Liss, Inc.

Original languageEnglish (US)
Pages (from-to)378-388
Number of pages11
JournalProteins: Structure, Function and Genetics
Issue number3
StatePublished - Aug 15 2000


  • Galectins
  • Lectin
  • N-acetyllactosamine
  • Thiodigalactose
  • X-ray diffraction

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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