Detailed Information on Publication Record
2012
Aspergillus fumigatus lectin - a model system for the study of multivalent lectins
KOMÁREK, Jan, Josef HOUSER, Marie POKORNÁ, Nikola KOSTLÁNOVÁ, Anne IMBERTY et. al.Basic information
Original name
Aspergillus fumigatus lectin - a model system for the study of multivalent lectins
Authors
KOMÁREK, Jan (203 Czech Republic), Josef HOUSER (203 Czech Republic), Marie POKORNÁ (203 Czech Republic), Nikola KOSTLÁNOVÁ (203 Czech Republic), Anne IMBERTY (250 France) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution)
Edition
Struktura a interakce biomolekul II, 2012
Other information
Language
English
Type of outcome
Konferenční abstrakt
Field of Study
10600 1.6 Biological sciences
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
RIV identification code
RIV/00216224:14310/12:00057369
Organization unit
Faculty of Science
Keywords (in Czech)
Aspergillus fumigatus; lektiny
Keywords in English
Aspergillus fumigatus; lectins
Změněno: 26/4/2012 13:39, Mgr. Jan Komárek, Ph.D.
Abstract
V originále
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.
Links
GD301/09/H004, research and development project |
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