1LGB

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

1LGB の概要

• エントリーDOI: 10.2210/pdb1lgb/pdb
• 分子名称: LEGUME ISOLECTIN II (ALPHA CHAIN), LEGUME ISOLECTIN II (BETA CHAIN), LACTOTRANSFERRIN (N2 FRAGMENT), ... (6 entities in total)
• 機能のキーワード: complex(lectin-transferrin), complex(lectin-transferrin) complex, complex(lectin/transferrin)
• 由来する生物種: Lathyrus ochruss (Yellow-flowered pea); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44980.55

構造登録者

Bourne, Y.,Cambillau, C. (登録日: 1994-01-07, 公開日: 1994-08-31, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.3 Å)