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PDBsum entry 4d4u

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Sugar binding protein PDB id
4d4u
Contents
Protein chains
314 a.a.
Ligands
NAG-GAL-FUC ×4
NDG-GAL-FUC-FUC ×3
GAL-FUC
GOL ×2
FUC ×2
Waters ×412

References listed in PDB file
Key reference
Title Structural insights into aspergillus fumigatus lectin specificity: afl binding sites are functionally non-Equivalent.
Authors J.Houser, J.Komarek, G.Cioci, A.Varrot, A.Imberty, M.Wimmerova.
Ref. Acta Crystallogr D Biol Crystallogr, 2015, 71, 442-453. [DOI no: 10.1107/S1399004714026595]
PubMed id 25760594
Abstract
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.
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