Engineering of PA-IIL lectin from Pseudomonas aeruginosa - Unravelling the role of the specificity loop for sugar preference

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Title in English	ngineering of PA-IIL lectin from Pseudomonas aeruginosa - Unravelling the role of the specificity loop for sugar preference
Authors	ADAM Jan POKORNÁ Martina SABIN Charles MITCHELL Edward P. IMBERTY Anne WIMMEROVÁ Michaela
Year of publication	2007
Type	Article in Periodical
Magazine / Source	BMC Structural Biology
MU Faculty or unit	Faculty of Science
Citation
Field	Biochemistry
Keywords	lectin; pseudomonas aeruginosa; protein engineering; microcalorimetry;X-ray
Description	Mutagenesis of amino acids forming the specificity binding loop in PA-IIL allowed identification of one amino acid that is crucial for definition of the lectin sugar preference. Altering specificity loop amino acids causes changes in saccharide-binding preferences of lectins derived from PA-IIL, via creation or blocking possible binding interactions. This finding opens a gate towards protein engineering and subsequent protein design to refine the desired binding properties and preferences, an approach that could have strong potential for drug design.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Structure-function studies on lectins and adhesins from microbial patogens Structural biophysics of macromolecules