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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.

Crystal structure of fucose-specific lectin from Aleuria aurantia binding ligands at three of its five sugar recognition sites., Fujihashi M, Peapus DH, Kamiya N, Nagata Y, Miki K, Biochemistry. 2003 Sep 30;42(38):11093-9. PMID:14503859

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Categories: Aleuria aurantia | Fujihashi, M. | Kamiya, N. | Miki, K. | Nagata, Y. | Peapus, D H. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Lectin | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic