D 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

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
Název: BIOMOLEKULÁRNÍ CENTRUM
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum