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@article{1300635, author = {Houser, Josef and Komárek, Jan and Cioci, Gianluca and Varrot, Annabelle and Imberty, Anne and Wimmerová, Michaela}, article_location = {HOBOKEN}, article_number = {March}, doi = {http://dx.doi.org/10.1107/S1399004714026595}, keywords = {Aspergillus fumigatus; lectin; SPR; protein-saccharide complex; pathogen}, language = {eng}, issn = {1399-0047}, journal = {ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY}, title = {Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent}, url = {http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf}, volume = {71}, year = {2015} }
TY - JOUR ID - 1300635 AU - Houser, Josef - Komárek, Jan - Cioci, Gianluca - Varrot, Annabelle - Imberty, Anne - Wimmerová, Michaela PY - 2015 TI - Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent JF - ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY VL - 71 IS - March SP - 442-453 EP - 442-453 PB - WILEY-BLACKWELL SN - 13990047 KW - Aspergillus fumigatus KW - lectin KW - SPR KW - protein-saccharide complex KW - pathogen UR - http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf L2 - http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf N2 - 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. ER -
HOUSER, Josef, Jan KOMÁREK, Gianluca CIOCI, Annabelle VARROT, Anne IMBERTY and Michaela WIMMEROVÁ. Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent. \textit{ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY}. HOBOKEN: WILEY-BLACKWELL, 2015, vol.~71, March, p.~442-453. ISSN~1399-0047. Available from: https://dx.doi.org/10.1107/S1399004714026595.
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