Publication details

Changes of binding specificity and thermodynamical parameters of lectin from Chromobacterium violaceum - carbohydrate binding site mutagenesis in the position 97

Authors

DEJMKOVÁ Eva POKORNÁ Marie ALÁN Jan WIMMEROVÁ Michaela

Year of publication 2009
Type Article in Proceedings
Conference XIII. Setkání biochemiků a molekulárních biologů
MU Faculty or unit

Faculty of Science

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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