4C1Y

Crystal Structure of Fucose binding lectin from Aspergillus Fumigatus (AFL) in complex with b-methylfucoside

Summary for 4C1Y

• Entry DOI: 10.2210/pdb4c1y/pdb
• Descriptor: FUCOSE-SPECIFIC LECTIN FLEA, methyl beta-L-fucopyranoside, GLYCEROL, ... (7 entities in total)
• Functional Keywords: sugar binding protein, fucoside
• Biological source: ASPERGILLUS FUMIGATUS; More
• Total number of polymer chains: 4
• Total formula weight: 141054.32

Authors

Houser, J.,Komarek, J.,Kostlanova, N.,Lahmann, M.,Cioci, G.,Varrot, A.,Imberty, A.,Wimmerova, M. (deposition date: 2013-08-14, release date: 2014-08-27, Last modification date: 2023-12-20)

Primary citation

Houser, J.,Komarek, J.,Cioci, G.,Varrot, A.,Imberty, A.,Wimmerova, M.
Structural Insights Into Aspergillus Fumigatus Lectin Specificity: Afl Binding Sites are Functionally Non-Equivalent.
Acta Crystallogr.,Sect.D, 71:442-, 2015

PubMed 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.

PubMed: 25760594
DOI: 10.1107/S1399004714026595

Experimental method

X-RAY DIFFRACTION (2.23 Å)