Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

ISSN

1399-0047

e-ISSN

—

Svazek periodika

71

Číslo periodika v rámci svazku

March

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

442-453

Kód UT WoS článku

000351155400003

EID výsledku v databázi Scopus

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