CRACKING THE LECTIN CODE ; IN SILICO MODELING AND STRUCTURE-FUNCTIONAL STUDY OF PRINCIPLES DRIVING SUGAR PREFERENCE IN PAIIL FAMILY

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Authors

ADAM Jan KŘÍŽ Zdeněk PROKOP Martin CHATZIPAVLOU Thomais ZOTOS Petros KOČA Jaroslav WIMMEROVÁ Michaela

Year of publication 2009
Type Article in Proceedings
Conference FEBS Journal
MU Faculty or unit

Faculty of Science

Citation
Field Biochemistry
Keywords lectin engineering; molecular modeling; thermodynamics
Description INTRODUCTION Pseudomonas aeruginosa is an opportunistic human pathogen, a bacterium capable of attacking individuals with lowered immunity barriers. It is e.g. responsible for lethal complications in patients with cystic fibrosis. The PAIIL lectin (a C type fucose-preferring lectin with sugar binding mediated by two calcium ions), produced by the bacterium plays a crucial role in the host pathogen interaction. Similar lectin sequences were found in other bacteria, displaying distinct differences in preference despite only small differences in structure of binding site. In vitro and in silico mutants were constructed in order to analyze the principles driving the sugar preference. METHODS Molecular docking was performed using the AUTODOCK and DOCK software.
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