1LGB
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 1LGB
| Entry DOI | 10.2210/pdb1lgb/pdb |
| Descriptor | LEGUME ISOLECTIN II (ALPHA CHAIN), LEGUME ISOLECTIN II (BETA CHAIN), LACTOTRANSFERRIN (N2 FRAGMENT), ... (6 entities in total) |
| Functional Keywords | complex(lectin-transferrin), complex(lectin-transferrin) complex, complex(lectin/transferrin) |
| Biological source | Lathyrus ochruss (Yellow-flowered pea) More |
| Total number of polymer chains | 3 |
| Total formula weight | 44980.55 |
| Authors | Bourne, Y.,Cambillau, C. (deposition date: 1994-01-07, release date: 1994-08-31, Last modification date: 2024-10-23) |
| 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 Cited by 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: 8069634DOI: 10.1016/S0969-2126(00)00022-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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