CARB 76 |
| In eukaryotes, glycosylation is the most prominent form of post-translational modification, playing key roles in protein structure and solubility, host-pathogen interactions, and development. Despite their ubiquitous nature, the majority of glycans and glycoproteins remain structurally uncharacterized, and consequently defining structure-function relationships remain prohibitive. We credit this sluggish progress to the lack of functional experimental tools. Typical genetic approaches used to study nucleic acids and proteins are not amenable to glycans as they are not primary gene products. Instead small molecule and biochemical approaches must be used to identify and define glycan structure. Here we take two complementary approaches towards controlling the expression of mucin-type O-linked glycosylation. In the first, direct metabolic incorporation of unnatural sugars defines further elaboration, allowing us to induce or repress specific glycan formation. In the second approach, decoy glycans are used to absorb the enzymatic activity of glycosyl-transferases, resulting in the under-glycosylation. |
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Chemical Glycobiology Symposium
7:00 PM-9:00 PM, Tuesday, 12 September 2006 Moscone Center -- Hall D, Poster
Sci-Mix
Division of Carbohydrate Chemistry |