2003
Aleuria aurantia lectin displays novel binding mode for fucose. Crystal structure and ligand interaction of a new family of fucolectins.
WIMMEROVÁ, Michaela, Edward MITCHELL, Jean-Frederic SANCHEZ, Catherine GAUTIER, Hugues LORTAT-JACOB et. al.Základní údaje
Originální název
Aleuria aurantia lectin displays novel binding mode for fucose. Crystal structure and ligand interaction of a new family of fucolectins.
Autoři
WIMMEROVÁ, Michaela (203 Česká republika, garant), Edward MITCHELL (826 Velká Británie a Severní Irsko), Jean-Frederic SANCHEZ (250 Francie), Catherine GAUTIER (250 Francie), Hugues LORTAT-JACOB (250 Francie), Nechama GILBOA-GARBER (376 Izrael) a Anne IMBERTY (250 Francie)
Vydání
Grenoble, France, 12th European Carbohydrate Symposium, s. 93-93, 2003
Nakladatel
CERMAV-CNRS
Další údaje
Jazyk
angličtina
Typ výsledku
Stať ve sborníku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Francie
Utajení
není předmětem státního či obchodního tajemství
Kód RIV
RIV/00216224:14310/03:00008864
Organizační jednotka
Přírodovědecká fakulta
Klíčová slova anglicky
aleuria aurantia; lectin; crystal structure; fungi
Štítky
Příznaky
Mezinárodní význam
Změněno: 15. 11. 2006 11:39, prof. RNDr. Michaela Wimmerová, Ph.D.
Anotace
V originále
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 a six-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) [2]. As RSL is smaller (91 amino acid residues compared to 312 of AAL), only two typical internal repeats can be found in sequence. SPR studies demonstrated that RSL shares similar specificity as AAL but highly prefers alpha-Fuc1-2 linkage. [1] Fukumori, F., Takeuchi, N., Hagiwara, T., Ohbayashi, H., Endo, T., Kochibe, N., Nagata, Y., and Kobata, A J. Biochem. 107, 190-196 (1990) [2] Sudakevitz, D., Imberty, A., and Gilboa-Garber, N., J. Biochem. 132, 353-358 (2002)
Návaznosti
LN00A016, projekt VaV |
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