| Abstract
| - Aleuria aurantia possesses a fucose-specific lectin (AAL) that is widely used as a specificprobe for fucose. Fucosylated sugars often play pivotal roles in many cellular processes. We have determinedthe crystal structure of AAL at 2.24 Å resolution in complex with only three fucose molecules in its fivesugar binding sites of a six-fold β-propeller structure. Very recently, the structure of AAL has beenindependently 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 arginineconformation bound to fucose molecules plays an essential role in generating the difference in the affinityin the five binding sites. Binding models with a couple of saccharides based on biochemical assays suggestthat hydrophobic contacts also play important roles in AAL recognizing its ligand.
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