Cloning and expression of a novel UDP-GlcNAc:α-D-mannoside β,2-N- acetylglucosaminyltransferase homologous to UDP-GlcNAc:α-3-D-mannoside β1,2-N-acetylglucosaminyltransferase I Academic Article Article uri icon


MeSH Major

  • Cell Transformation, Viral
  • Epstein-Barr Virus Infections
  • Gastrointestinal Microbiome
  • Helicobacter Infections
  • Helicobacter pylori
  • Herpesvirus 4, Human
  • Stomach Neoplasms


  • The interplay between metal binding, carbohydrate binding activity, stability and structure of the lectin from Pterocarpus angolensis was investigated. Removal of the metals leads to a more flexible form of the protein with significantly less conformational stability. Crystal structures of this metal-free form show significant structural rearrangements, although some structural features that allow the binding of sugars are retained. We propose that substitution of an asparagine residue at the start of the C-terminal beta-strand of the legume lectin monomer hinders the trans-isomerization of the cis-peptide bond upon demetallization and constitutes an intramolecular switch governing the isomer state of the non-proline bond and ultimately the lectin phenotype.

publication date

  • January 2002



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1042/0264-6021:3610153

PubMed ID

  • 11742540

Additional Document Info

start page

  • 153

end page

  • 67


  • 361


  • 1