Publication details
High affinity lectins from human opportunistic pathogens: structure/function studies
| Authors | |
|---|---|
| Year of publication | 2007 |
| Type | Article in Proceedings |
| Conference | XIX International Symposium on Glycoconjugates |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | lectin; pathogen; x-ray structure; calorimetry |
| Description | The complementary techniques of binding experiments, isothermal titration microcalorimetry, surface plasmon resonance and high resolution X-ray crystallography were used to decipher the thermodynamical and structural basis for the unusually high affinity binding of these lectins to their host carbohydrates. In addition, site-directed mutagenesis in combination with structural and functional studies was used to understand the roles of particular amino acids in the fine definition of sugar specificity and preference. |
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