Structural highlights
1iub is a 1 chain structure with sequence from Aleuria aurantia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 2.31Å |
| Ligands: | , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN |
Function
LECF_ALEAU Might have a role in the differentiation of cells. Binds L-fucose.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fujihashi M, Peapus DH, Kamiya N, Nagata Y, Miki K. Crystal structure of fucose-specific lectin from Aleuria aurantia binding ligands at three of its five sugar recognition sites. Biochemistry. 2003 Sep 30;42(38):11093-9. PMID:14503859 doi:10.1021/bi034983z
