Aleuria aurantia lectin displays novel binding mode for fucose. Crystal structure and ligand interaction of a new family of fucolectins.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00008864" target="_blank" >RIV/00216224:14310/03:00008864 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Aleuria aurantia lectin displays novel binding mode for fucose. Crystal structure and ligand interaction of a new family of fucolectins.

Popis výsledku v původním jazyce

Aleuria aurantia lectin (AAL) is a fungal protein that specifically recognised fucose moiety in glycans. The crystal structure of AAL complexed with fucose has been solved at 1.5 A resolution. AAL displays a dimer composition, each subunit consists of asix-bladed beta-propeller fold and of a small antiparallel two-strands beta-sheet that play a role in dimerization. Primary sequence of AAL contains six internal repeats [1] corresponded to particular blades, crystal structure reveals five fucose molecules per AAL monomer in binding sites formed by two adjacent blades. Surface plasmon resonance experiments have been performed on a series of fucose containing oligosaccharides to determine equilibrium dissociation constants for lectine-oligosaccharide interaction. Measurements confirm the broad specificity of the lectin, with a slight preference for alpha-Fuc1-2Gal disaccharide. AAL shows high sequence similarity with a lectin from plant pathogenic bacterium Ralstonia solanacearum (RSL) [

Název v anglickém jazyce

Aleuria aurantia lectin displays novel binding mode for fucose. Crystal structure and ligand interaction of a new family of fucolectins.

Popis výsledku anglicky

Aleuria aurantia lectin (AAL) is a fungal protein that specifically recognised fucose moiety in glycans. The crystal structure of AAL complexed with fucose has been solved at 1.5 A resolution. AAL displays a dimer composition, each subunit consists of asix-bladed beta-propeller fold and of a small antiparallel two-strands beta-sheet that play a role in dimerization. Primary sequence of AAL contains six internal repeats [1] corresponded to particular blades, crystal structure reveals five fucose molecules per AAL monomer in binding sites formed by two adjacent blades. Surface plasmon resonance experiments have been performed on a series of fucose containing oligosaccharides to determine equilibrium dissociation constants for lectine-oligosaccharide interaction. Measurements confirm the broad specificity of the lectin, with a slight preference for alpha-Fuc1-2Gal disaccharide. AAL shows high sequence similarity with a lectin from plant pathogenic bacterium Ralstonia solanacearum (RSL) [

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

Návaznosti

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

Rok uplatnění

2003

Kód důvěrnosti údajů

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

Název statě ve sborníku

12th European Carbohydrate Symposium

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

93

Název nakladatele

CERMAV-CNRS

Místo vydání

Grenoble, France

Místo konání akce

Grenoble, France

Datum konání akce

1. 1. 2003

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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