CARB 17 |
| The Siglec family of cell adhesion proteins comprise a subfamily of the immunoglobulin superfamily with variable numbers of extracellular Ig domains including a unique, homologous N-terminal Ig domain, the sialic acid binding domain. The cytoplasmic domains of the siglecs typically contain one or more tyrosine based 'ITIM' motifs characteristic of accessory proteins that regulate transmembrane signaling of cell surface receptor proteins. One of our approaches to dissect the biology of the siglecs is to employ novel carbohydrate probes that modulate their function. We use chemo-enzymatic approaches to synthesize sialoside analogs recognized by siglecs. Their utility ranging from potent mono- or multivalent probes to monovalent sialic acid analogs that can be fed to cells and incorporated into cell surface glycoproteins to add chemical functionality or alter the affinity of sialoside ligands for binding cell surface siglecs. This presentation will cover synthetic strategies, screening of sialoside inhibitors and their use as biological probes for investigating roles of siglecs in cell signaling. |
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Carbohydrate Recognition Mechanisms and Applications
2:00 PM-4:30 PM, Monday, 27 March 2006 Georgia World Congress Center -- B409, Oral
Division of Carbohydrate Chemistry |