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Aspergillus fumigatus lectin - a model system for the study of multivalent lectins

Basic information
Original title:Aspergillus fumigatus lectin - a model system for the study of multivalent lectins
Authors:Jan Komárek, Josef Houser, Marie Pokorná, Nikola Kostlánová, Anne Imberty, Michaela Wimmerová
Further information
Citation:KOMÁREK, Jan, Josef HOUSER, Marie POKORNÁ, Nikola KOSTLÁNOVÁ, Anne IMBERTY and Michaela WIMMEROVÁ. Aspergillus fumigatus lectin - a model system for the study of multivalent lectins. In Struktura a interakce biomolekul II. 2012.Export BibTeX
@proceedings{980537,
author = {Komárek, Jan and Houser, Josef and Pokorná, Marie and Kostlánová, Nikola and Imberty, Anne and Wimmerová, Michaela},
booktitle = {Struktura a interakce biomolekul II},
keywords = {Aspergillus fumigatus; lectins},
language = {eng},
title = {Aspergillus fumigatus lectin - a model system for the study of multivalent lectins},
year = {2012}
}
Original language:English
Field:Biochemistry
Type:Conference abstract
Keywords:Aspergillus fumigatus; lectins

Lectins are sugar-specific proteins involved in recognition events in a variety of physiological and pathological processes. The project is focused on a detailed characterization of L-fucose specific lectin AFL from ascomycete Aspergillus fumigatus. Structure-function studies of AFL revealed presence of six binding sites with different affinities and specificities towards fucosylated oligosaccharides. Detailed knowledge of differences in binding properties of individual AFL binding sites would be important in understanding the basis of protein-carbohydrate recognition. Further study is therefore needed to examine the fine details in behaviour of different AFL binding sites. This study uses a novel approach which is based on a synthetic gene and site-directed mutagenesis. The procedure should result in preparation of six monovalent forms of AFL (corresponding to individual binding sites) and their characterization from structure-function point of view.

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