Classification of Glycan Binding Proteins

Glycans can mediate a wide variety of biological roles by virtue of their mass, shape, charge, or other physical properties. However, many of their more specific biological roles are mediated via recognition by GBPs. Nature appears to have taken full advantage of the vast diversity of glycans expressed in organisms by evolving protein modules to recognize discrete glycans that mediate specific physiological or pathological processes. Excluding glycan-specific antibodies, GBPs broadly into two major groups such as lectins and glycosaminoglycan-binding proteins. Most lectins are members of families with defined “carbohydrate-recognition domains” (CRDs) that apparently evolved from shared ancestral genes, often retaining specific features of primary amino acid sequence or three-dimensional structure. Thus, new family members can be identified by searching protein sequence or structural databases. The natural ligands for most lectins are typically complex glycoconjugates that carry clustered arrays of the cognate carbohydrate or unique glycan structures, thus cooperating with clustered lectin-binding sites to generate high-avidity binding, which is further enhanced by mass transport effects (high local concentrations of ligands).

Relevant Conferences:Glycobiology Conferences Biochemistry Conferences

6th International Conference on Bioinformatics, March 29-30, 2016 Valencia, Spain; International Conference on Structural Biology, June 23-24, 2016 New Orleans, USA; World Congress on Amino Acids and Proteins, December 08-09, 2016 Baltimore, USA; International Conference on Nucleic Acids, August 04-06, 2016 Seattle, USA 7th International Conference and Expo on Proteomics, October 24-26, 2016 Rome, Italy; International Conference on Obesity & Chronic Diseases, July 25-27, 2016 Las Vegas USA; International Conference on New Therapeutics for Diabetes and Obesity, April 17-20, 2016 La Jolla, USA; Conference on Plasma Spectrochemistry, January 10-16, 2016 Tucson, USA; Euro Fed Lipid Congress, September 18-21, 2016 Gent, Belgium; Conference on Obesity and Adipose Tissue Biology, February 15-19, 2016 Banff, Canada

Complex carbohydrates are composed of monosaccharides that are covalently linked by glycosidic bonds, either in the α or β form. Unlike DNA and proteins, however monosaccharides may be linked to one or more other monosaccharides, such that they form a branched tree structure. Glyco arrays and the specific subject of protein binding to immobilized glycans, is a current focus of active research involving several individual strategies in terms of chemistries and choice of glycan ligand. This new technology shows considerable promise to investigate the biological significance of glycan sequences. Such information has proved to be difficult to screen in the past and demands a high-throughput solution. The complex structure of glycans has been a bottleneck in the structure determination and thus data accumulation of glycan structures. 

  • Carbohydrate recognition domains
  • Glycan Array modelling structure
  • Sugar binding proteins
  • Protein trafficking
  • Ligand profiling
  • Glycosaminoglycan binding proteins

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