Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00080833" target="_blank" >RIV/00216224:14740/15:00080833 - isvavai.cz</a>
Result on the web
<a href="http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf" target="_blank" >http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1107/S1399004714026595" target="_blank" >10.1107/S1399004714026595</a>
Alternative languages
Result language
angličtina
Original language name
Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent
Original language description
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 ofstructures 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 owingto 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 humanepithelia. 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 ap
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN
1399-0047
e-ISSN
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Volume of the periodical
71
Issue of the periodical within the volume
March
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
442-453
UT code for WoS article
000351155400003
EID of the result in the Scopus database
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