Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety.
Bourne, Y., Mazurier, J., Legrand, D., Rouge, P., Montreuil, J., Spik, G., Cambillau, C.(1994) Structure 2: 209-219
- PubMed: 8069634 
- DOI: https://doi.org/10.1016/s0969-2126(00)00022-8
- Primary Citation of Related Structures:  
1LGB, 1LGC - PubMed Abstract: 
Lectins mediate cell-cell interactions by specifically recognizing oligosaccharide chains. Legume lectins serve as mediators for the symbiotic interactions between plants and nitrogen-fixing microorganisms, an important process in the nitrogen cycle. Lectins from the Viciae tribe have a high affinity for the fucosylated biantennary N-acetyllactosamine-type glycans which are to be found in the majority of N-glycosylproteins. While the structures of several lectins complexed with incomplete oligosaccharides have been solved, no previous structure has included the complete glycoprotein.
Organizational Affiliation: 
Laboratoire de Cristallographie et de Cristallisation des Macromolécules Biologiques, CNRS URA 1296, Faculté de Médecine Secteur-Nord, Marseille, France.