Detailed Information on Publication Record
2007
UNRAVELING THE PROBLEMS OF PROTEIN - SACCHARIDE INTERACTIONS VIA COMPUTATIONAL CHEMISTRY
KŘÍŽ, Zdeněk, Jan ADAM, Ondřej ŠULÁK, Michaela WIMMEROVÁ, Jaroslav KOČA et. al.Basic information
Original name
UNRAVELING THE PROBLEMS OF PROTEIN - SACCHARIDE INTERACTIONS VIA COMPUTATIONAL CHEMISTRY
Name in Czech
Řešení problémů interakcí protein - sacharid s použitím metod počítačové chemie
Authors
Edition
Materials structure, Czech Republic, Czech and Slovak Crystallographic Associ, 2007, 1211-5894
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10403 Physical chemistry
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
Organization unit
Faculty of Science
Keywords in English
computational chemistry;computer modeling;docking;
Tags
International impact, Reviewed
Změněno: 17/6/2008 08:46, Mgr. Zdeněk Kříž, Ph.D.
V originále
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.
In Czech
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.
Links
| GA303/06/0570, research and development project |
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| GD204/03/H016, research and development project |
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| LC06030, research and development project |
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| MSM0021622413, plan (intention) |
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