4d52

CRYSTAL STRUCTURE OF FUCOSE BINDING LECTIN FROM ASPERGILLUS FUMIGATUS (AFL) IN COMPLEX WITH L-GALACTOPYRANOSE.

spinqualitylabelsall models 4d52, resolution 1.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d52 is a 4 chain structure with sequence from Aspergillus fumigatus. This structure supersedes the now removed PDB entries 4uq7 and 4ahb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.76Å Ligands: CSD, GIV, GXL, NA, PEG, PG4, PGE, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LECF_ASPFU Multispecific lectin that is able to recognize L-fucose in all possible linkages (PubMed:23695231, PubMed:27058347, PubMed:24340081, PubMed:25760594). These could be found not only in decomposed plant matter in soil, which is the natural environment for A.fumigatus, but also in various epitopes on human tissues (PubMed:25760594). Mediates binding of A.fumigatus conidia to airway mucinin a fucose dependent manner (PubMed:27058347). Stimulates IL-8 production by human bronchial cells in a dose-dependent manner, contributing to the inflammatory response observed upon the exposure of a patient to A.fumigatus, and thus might be an important virulence factor involved in an early stage of A.fumigatus infection (PubMed:24340081). 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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