Stereochemical basis of high affinity of Pseudomonas aeruginosa lectin for fucose : structural and thermodynamic characterisation

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00008871" target="_blank" >RIV/00216224:14310/03:00008871 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Stereochemical basis of high affinity of Pseudomonas aeruginosa lectin for fucose : structural and thermodynamic characterisation
Original language description
Human pathogenic bacterium Pseudomonas aeruginosa, which is a major cause of mortality and morbidity of cystic fibrosis patients, produces fucose-binding lectin (PA-IIL) that highly contributes to the pathogen virulence.The crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A [1] and additional experiments have been performed in order to understand the molecular basis of both specificity and affinity of PA-IIL for monosaccharides. Crystals have been obtained for the protein complexed with b-Me-D-arabinopyranoside and L-galactose and structures were solved by molecular replacement. Co-crystallisation of the lectin with trisaccharides of the Lea and Lex family is being in progress.Isothermal titration microcalorimetry experiments ona series of monosaccharides sharing similar stereochemical three-hydroxyl arrangement needed for recognition were performed in order to characterize the thermodynamic parameters of the carbohydrate-lectin interaction. The stereochemical
Czech name
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Czech description
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Project
<a href="/en/project/ME%20675" target="_blank" >ME 675: Structural-functional study of bacterial viruses lectins.</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2003
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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