1iuc
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(New page: 200px<br /><applet load="1iuc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iuc, resolution 2.24Å" /> '''Fucose-specific lect...)
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Revision as of 15:33, 20 November 2007
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Fucose-specific lectin from Aleuria aurantia with three ligands
Overview
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.
About this Structure
1IUC is a Single protein structure of sequence from Aleuria aurantia with FUL, FUC and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
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
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