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X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution

J Biol Chem. 1998 May 22;273(21):13047-52. doi: 10.1074/jbc.273.21.13047.

Abstract

Galectins are a family of lectins which share similar carbohydrate recognition domains (CRDs) and affinity for small beta-galactosides, but which show significant differences in binding specificity for more complex glycoconjugates. We report here the x-ray crystal structure of the human galectin-3 CRD, in complex with lactose and N-acetyllactosamine, at 2.1-A resolution. This structure represents the first example of a CRD determined from a galectin which does not show the canonical 2-fold symmetric dimer organization. Comparison with the published structures of galectins-1 and -2 provides an explanation for the differences in carbohydrate-binding specificity shown by galectin-3, and for the fact that it fails to form dimers by analogous CRD-CRD interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens, Differentiation / chemistry
  • Antigens, Differentiation / metabolism*
  • Binding Sites
  • Carbohydrate Metabolism*
  • Crystallography, X-Ray
  • Dimerization
  • Galectin 1
  • Galectin 2
  • Galectin 3
  • Hemagglutinins / chemistry
  • Humans
  • Models, Molecular

Substances

  • Antigens, Differentiation
  • Galectin 1
  • Galectin 2
  • Galectin 3
  • Hemagglutinins

Associated data

  • PDB/1A3K