Crystal Structure of Fucose-Specific Lectin from Aleuria aurantia Binding Ligands at Three of Its Five Sugar Recognition Sites,

Citations Over TimeTop 23% of 2003 papers

Abstract

Aleuria aurantia possesses a fucose-specific lectin (AAL) that is widely used as a specific probe for fucose. Fucosylated sugars often play pivotal roles in many cellular processes. We have determined the crystal structure of AAL at 2.24 A resolution in complex with only three fucose molecules in its five sugar binding sites of a six-fold beta-propeller structure. Very recently, the structure of AAL has been independently determined, showing that all the five binding sites were occupied by fucose molecules [Wimmerova, M., et al. (2003) J. Biol. Chem. 278, 27059-27067]. Stabilization of the arginine conformation bound to fucose molecules plays an essential role in generating the difference in the affinity in the five binding sites. Binding models with a couple of saccharides based on biochemical assays suggest that hydrophobic contacts also play important roles in AAL recognizing its ligand.

Related Papers

• → On the biosynthesis of L-fucose and L-fucose metabolism in man(1960)32 cited
• → 2-Deoxy-2-fluoro-L-fucose and its effect on L-[1-14C] fucose utilization in mammalian cells(1979)18 cited
• Clinical significance of fucose level in glycoprotein fraction of serum in patients with malignant tumors.(1977)
• → Novel fucose-containing components from rat tissues(1977)12 cited
• → The Determination of Fucose in Complex Natural Products(1972)