Effect of glycosylation on the structure of Erythrina corallodendron lectin

Proteins. 2004 Sep 1;56(4):821-7. doi: 10.1002/prot.20168.


The three-dimensional structure of the recombinant form of Erythrina corallodendron lectin, complexed with lactose, has been elucidated by X-ray crystallography at 2.55 A resolution. Comparison of this non-glycosylated structure with that of the native glycosylated lectin reveals that the tertiary and quaternary structures are identical in the two forms, with local changes observed at one of the glycosylation sites (Asn17). These changes take place in such a way that hydrogen bonds with the neighboring protein molecules in rECorL compensate those made by the glycan with the protein in ECorL. Contrary to an earlier report, this study demonstrates that the glycan attached to the lectin does not influence the oligomeric state of the lectin. Identical interactions between the lectin and the non-covalently bound lactose in the two forms indicate, in line with earlier reports, that glycosylation does not affect the carbohydrate specificity of the lectin. The present study, the first of its kind involving a glycosylated protein with a well-defined glycan and the corresponding deglycosylated form, provides insights into the structural aspects of protein glycosylation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Validation Study

MeSH terms

  • Binding Sites
  • Carbohydrate Metabolism
  • Crystallography, X-Ray
  • Glycosylation
  • Lactose / chemistry
  • Lactose / metabolism
  • Lectins / chemistry
  • Lectins / metabolism
  • Plant Lectins / chemistry*
  • Plant Lectins / metabolism*
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism


  • Lectins
  • Plant Lectins
  • Recombinant Proteins
  • erythrina lectin
  • Lactose