ADAM, Jan, Martina POKORNÁ, Charles SABIN, Edward P. MITCHELL, Anne IMBERTY and Michaela WIMMEROVÁ. Engineering of PA-IIL lectin from Pseudomonas aeruginosa - Unravelling the role of the specificity loop for sugar preference (ngineering of PA-IIL lectin from Pseudomonas aeruginosa - Unravelling the role of the specificity loop for sugar preference). BMC Structural Biology. 2007, vol. 7, No 36, p. 1-13. ISSN 1472-6807.
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Basic information
Original name Engineering of PA-IIL lectin from Pseudomonas aeruginosa - Unravelling the role of the specificity loop for sugar preference
Name in Czech Proteinove inzenyrstvi lektinu PA-IIL z Pseudomonas aeruginosa: uloha aminokyselin odpovidajicich za specifitu
Authors ADAM, Jan (203 Czech Republic), Martina POKORNÁ (203 Czech Republic), Charles SABIN (250 France), Edward P. MITCHELL (826 United Kingdom of Great Britain and Northern Ireland), Anne IMBERTY (250 France) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor).
Edition BMC Structural Biology, 2007, 1472-6807.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14310/07:00020277
Organization unit Faculty of Science
UT WoS 000247687500001
Keywords in English lectin; pseudomonas aeruginosa; protein engineering; microcalorimetry;X-ray
Tags lectin, microcalorimetry, Protein engineering, Pseudomonas aeruginosa, x-ray
Tags International impact, Reviewed
Changed by Changed by: Ing. et Ing. Jan Adam, Ph.D., učo 151533. Changed: 23/6/2008 08:36.
Abstract
Mutagenesis of amino acids forming the specificity binding loop in PA-IIL allowed identification of one amino acid that is crucial for definition of the lectin sugar preference. Altering specificity loop amino acids causes changes in saccharide-binding preferences of lectins derived from PA-IIL, via creation or blocking possible binding interactions. This finding opens a gate towards protein engineering and subsequent protein design to refine the desired binding properties and preferences, an approach that could have strong potential for drug design.
Abstract (in Czech)
Mutageneze aminokyselin vazebneho mista PA-IIL lektinu ukazala vyznam jednotlivych rezidui pro specifitu proteinu.
Links
GA303/06/0570, research and development projectName: Strukturně-funkční studie lektinů a adhezinů patogenních mikroorganismů
Investor: Czech Science Foundation, Structure-function studies on lectins and adhesins from microbial patogens
GD204/03/H016, research and development projectName: Strukturní biofyzika makromolekul
Investor: Czech Science Foundation, Structural biophysics of macromolecules
MSM0021622413, plan (intention)Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
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