UNRAVELING THE PROBLEMS OF PROTEIN - SACCHARIDE INTERACTIONS VIA COMPUTATIONAL CHEMISTRY

Investor logo
Investor logo

Warning

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

KŘÍŽ Zdeněk ADAM Jan ŠULÁK Ondřej WIMMEROVÁ Michaela KOČA Jaroslav

Year of publication 2007
Type Article in Periodical
Magazine / Source Materials structure
MU Faculty or unit

Faculty of Science

Citation
Web
Field Physical chemistry and theoretical chemistry
Keywords computational chemistry;computer modeling;docking;
Description Detailed knowledge of interactions between proteins and small molecules is important for understanding of signifi- cant processes in organisms. Saccharides and various glycoconjugates play a significant role in many host-patho- gen interactions. Lectins are sugar-binding proteins of non-immunoglobulin nature that agglutinate cells or pre- cipitate glycoconjugates. Their specificity is usually de- fined by the monosaccharides or oligosaccharides that are best at inhibiting the agglutination or precipitation the lectin causes. Lectins are of interest because of their wide variety of properties and potential applications (pharma- cology, immunology, cancer therapy, agriculture ...). Since host carbohydrates have been known for many years to constitute specific attachment sites for pathogen protein receptors, there is a great interest in structure-func- tion studies of bacterial proteins enabling the pathogen at- tachment to host glycans. However, only a limited number of their complexes with receptors have been characterizedby crystallography [1]. The molecular modeling methods can help in the study of the complexes. The study will be focused on docking of a set of monosaccharides into two different lectins originally from bacteria Pseudomonas aeruginosa (PA-IIL) [2] and Ralstonia solanacearum (RS-20L) using the Dock v. 6.0 program.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.

More info