In vitro and in silico protein engineering of lectins
| Authors | |
|---|---|
| Year of publication | 2007 |
| Type | Article in Proceedings |
| Conference | 14th European Carbohydrate Symposium, EUROCARB 14 |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | mutagenesis; structure; lectin; pathogen |
| Description | The contribution is focused on bacterial lectins from human opportunistic pathogens, which display sub-micromolar range affinity towards their carbohydrate ligands, targeting specially proteins from bacteria dangerous for cystic fibrosis patients. The combination of binding experiments (isothermal titration microcalorimetry, surface plasmon resonance,...) and X-ray crystallography approaches is used to decipher the thermodynamical and structural basis for high affinity binding of these lectins to host carbohydrates. Site-directed mutagenesis in combination with structural and functional studies is used to understandthe role of particular amino acids for sugar specificity and preference. In order to explore these interesting features deeper, we have been using a computational chemistry approach with the graphic program TRITON that is being under development at our institute. TRITON automates in silico engineering of proteins by generation of desired mutant proteins and performs docking experiments using AUTODOCK [2]. The TRITON results are correlated with experimental data. |
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