4agt

Crystal Structure of Fucose binding lectin from Aspergillus Fumigatus (AFL) in complex with Fuc1-6GlcNAc.

spinqualitylabelsall models 4agt, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4agt is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FUC, NA, NAG, NDG Related: 4agi Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The Aspergillus fumigatus lectin AFL was recently described as a new member of the AAL lectin family. As a lectin from an opportunistic pathogen, it might play an important role in the interaction of the pathogen with the human host. A detailed study of structures of AFL complexed with several monosaccharides and oligosaccharides, including blood-group epitopes, was combined with affinity data from SPR and discussed in the context of previous findings. Its six binding sites are non-equivalent, and owing to minor differences in amino-acid composition they exhibit a marked difference in specific ligand recognition. AFL displays a high affinity in the micromolar range towards oligosaccharides which were detected in plants and also those bound on the human epithelia. All of these results indicate AFL to be a complex member of the lectin family and a challenging target for future medical research and, owing to its binding properties, a potentially useful tool in specific biotechnological applications. Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent.,Houser J, Komarek J, Cioci G, Varrot A, Imberty A, Wimmerova M Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):442-53. doi:, 10.1107/S1399004714026595. Epub 2015 Feb 26. PMID:25760594 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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