Publication details
Changes of binding specificity and thermodynamical parameters of lectin from Chromobacterium violaceum - carbohydrate binding site mutagenesis in the position 97
Authors | |
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Year of publication | 2009 |
Type | Article in Proceedings |
Conference | XIII. Setkání biochemiků a molekulárních biologů |
MU Faculty or unit | |
Citation | |
Field | Biochemistry |
Keywords | Lectins; Chromobacterium violaceum; changes of binding properties |
Description | CV-IIL is lectin from human opprotunistic pathogen Chromobacterium violaceum. The aim of this work is a construction of mutant lectins by changing amino acid threonine in the position 97 of carbohydrate binding site. The crystal structure of the CV-IIL lectin shows, that amino acid threonin in position 97 is bound to monosaccharide through one watter molecule. Substitution of this amino acid should lead to changes of sugar binding properties, that could be determinate by the method surface plasmon resonance and isothermal titration microcalorimetry. |
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