Structural basis of the affinity for oligomannosides and analogs displayed by BC2L-A, a Burkholderia cenocepacia soluble lectin

Warning

This publication doesn't include Institute of Computer Science. It includes Faculty of Science. Official publication website can be found on muni.cz.

Authors	LAMEIGNERE Emilie SHIAO Tze Chieh ROY Rene WIMMEROVÁ Michaela DUBREUIL Fréderic VARROT Annabelle IMBERTY Anne
Year of publication	2009
Type	Article in Periodical
Magazine / Source	Glycobiology
MU Faculty or unit	Faculty of Science
Citation
Field	Biophysics
Keywords	bacterial lectin;Burkholderia cenocepacia;mannose;oligosaccharides
Description	The disaccharides and the trisaccharide,Man1-3(Man1-6)Man were tested by titration microcalorimetry in order to evaluate their affinity for BC2L-A in solution and to characterize the thermodynamics of the binding. Oligomannose analogs presenting two mannoside residues separated by either flexible or rigid spacer where also tested.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Biomolecular centre Design of Carbohydrates and Glycomimetics as Antibacterial and Antiviral Drugs Lectins from human pathogens - structure, function, engineering