Over the past three decades the field of glycobiology has expanded beyond a basic understanding of the structure and biosynthesis of glycoprotein, proteoglycans, and glycolipids toward a more detailed picture of how these molecules afford communication through binding to mammalian lectins. Although the number of different mammalian lectin domains appears to be finite and even much smaller than early estimates predicated based on the diversity of glycan structures, nature appears capable of using these in numerous combinations to fine tune specificity. The following provides an overview of the major classes of mammalian lectins and discusses their glycan binding specificity. The review provides a snapshot of the field of glycobiology that continues to grow providing an increasing number of examples of biological processes that rely upon glycan-lectin binding.
CITATION STYLE
Anderson, K., Evers, D., & Rice, K. G. (2008). Structure and Function of Mammalian Carbohydrate-Lectin Interactions. In Glycoscience (pp. 2445–2482). Springer Berlin Heidelberg. https://doi.org/10.1007/978-3-540-30429-6_63
Mendeley helps you to discover research relevant for your work.