Engineering of PA-IIL lectin from Pseudomonas aeruginosa - Unravelling the role of the specificity loop for sugar preference

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.

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

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Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

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

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Abstract

V originále

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.

In Czech

Mutageneze aminokyselin vazebneho mista PA-IIL lektinu ukazala vyznam jednotlivych rezidui pro specifitu proteinu.

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Links

GA303/06/0570, research and development project	Name: 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 project	Name: 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