Structural basis for the recognition of carbohydrates by human galectin-7

Biochemistry. 1998 Oct 6;37(40):13930-40. doi: 10.1021/bi981056x.


Knowledge about carbohydrate recognition domains of galectins, formerly known as S-type animal lectins, is important in understanding their role(s) in cell-cell interactions. Here we report the crystal structure of human galectin-7 (hGal-7), in free form and in the presence of galactose, galactosamine, lactose, and N-acetyl-lactosamine at high resolution. This is the first structure of a galectin determined in both free and carbohydrate-bound forms. The structure shows a fold similar to that of the prototype galectins -1 and -2, but has greater similarity to a related galectin molecule, Gal-10. Even though the carbohydrate-binding residues are conserved, there are significant changes in this pocket due to shortening of a loop structure. The monomeric hGal-7 molecule exists as a dimer in the crystals, but adopts a packing arrangement considerably different from that of Gal-1 and Gal-2, which has implications for carbohydrate recognition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Sugars / metabolism
  • Animals
  • Binding Sites
  • Carbohydrate Metabolism*
  • Cattle
  • Crystallization
  • Crystallography, X-Ray
  • Galactosamine / metabolism
  • Galactose / metabolism
  • Galectins*
  • Humans
  • Lactose / metabolism
  • Lectins / chemistry*
  • Lectins / isolation & purification
  • Lectins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Structure-Activity Relationship


  • Amino Sugars
  • Galectins
  • LGALS7 protein, human
  • Lectins
  • N-acetyllactosamine
  • Galactosamine
  • Lactose
  • Galactose

Associated data

  • PDB/1BKZ
  • PDB/2GAL
  • PDB/3GAL
  • PDB/4GAL
  • PDB/5GAL