1LGC

INTERACTION OF A LEGUME LECTIN WITH THE N2 FRAGMENT OF HUMAN LACTOTRANSFERRIN OR WITH THE ISOLATED BIANTENNARY GLYCOPEPTIDE: ROLE OF THE FUCOSE MOIETY

Summary for 1LGC

• Entry DOI: 10.2210/pdb1lgc/pdb
• Descriptor: LEGUME ISOLECTIN II (ALPHA CHAIN), DIPEPTIDE, LEGUME ISOLECTIN II (BETA CHAIN), ... (9 entities in total)
• Functional Keywords: lectin
• Biological source: Lathyrus ochrus (yellow-flowered pea)
• Total number of polymer chains: 9
• Total formula weight: 83759.83

Authors

Bourne, Y.,Cambillau, C. (deposition date: 1994-01-07, release date: 1994-08-31, Last modification date: 2020-07-29)

Primary citation

Bourne, Y.,Mazurier, J.,Legrand, D.,Rouge, P.,Montreuil, J.,Spik, G.,Cambillau, C.
Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety.
Structure, 2:209-219, 1994

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.

PubMed: 8069634
DOI: 10.1016/S0969-2126(00)00022-8

Experimental method

X-RAY DIFFRACTION (2.8 Å)