Glycan Component Classification
The term ‘glycobiology’, introduced in 1988, focused attention on the role of oligosaccharides in the context of the proteins to which they were attached. Glycans can affect the physical properties of the proteins to which they are attached and provide lectin-recognition sites. Thus, roles for glycosylation have been shown in protein folding in the endoplasmic reticulum, transport and secretion, anchoring of proteins and protease protection. It is now becoming apparent that glycans can also have a direct structural role, affecting the tertiary or quaternary fold of the protein.
Fig.1 Chemical diversity of glycans. (Raman, 2005)
Glycan Component Classification
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Name
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Introduction
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N-Glycans
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N-glycan is a specific type of glycan linked to asparagine (Asn, N) in the sequence Asn-X-Ser/Thr where X can be any amino acid except proline (Pro, P). N-glycan structure affects pharmacokinetics, pharmacodynamics and immunogenicity, and is the most widely known form of glycosylation in biopharmaceuticals.
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O-Glycans
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Modification of serine or threonine residues on proteins by linking GalNAc residues produces O-glycans
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GPI-anchored glycoprotein
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Glycosylphosphatidy-inositol-anchored glycoprotein (GPI-anchored glycoprotein) is a type of glycoprotein that is anchored to the cell membrane surface through its hydroxyl-terminal GPI structure without spanning its phospholipid bilayer structure. It is involved in important life processes such as cells recognition, growth, regeneration, programmed death, etc.
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Glycosphingolipid
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Glycosphingolipid is an amphiphilic molecule formed by the glycosidic bond of ceramide and oligosaccharide chain, and is a component of eukaryotic cell membrane. Glycosphingolipids are involved in cell-to-cell communication and can be used as antigenic determinants of the ABO blood group, as well as receptors for viruses and bacterial toxins.
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Glycosaminoglycans and Proteoglycans
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Glycosaminoglycans are large linear polysaccharides composed of repeating disaccharide units. Its main configuration contains amino sugars and uronic acid (glucuronic acid and/or iduronic acid), and is the main component of the extracellular matrix. Proteoglycan is a kind of glycoconjugate composed of core protein and one or more covalently linked glycosaminoglycans. Its molecules usually contain more than 50% sugar.
Glycosaminoglycans and Proteoglycans are important component of cell membrane, basement membrane, especially extracellular matrix, and is closely related to the structure and function of tissue cells.
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Services at Creative Biolabs
Glycans are of great importance within eukaryotes performing a variety of functions associated with cellular metabolism needed for protein synthesis, movement and transport. Glycosylation is the most common post translational modification in eukaryotes linking carbohydrates to proteins, nucleic acids, cell surfaces, secreted soluble molecules and other macromolecules. Depending on the arrangement of carbohydrate moieties covalently linked to specific regions of these macromolecules, classes of these glycans can be derived. Each glycan performs vital and diverse roles in protein activity and conformation.
Creative Biolabs is a world-class supplier of glycan synthesis, providing a full range of Custom Glycan Synthesis. If you have any questions about glycan synthesis, please do not hesitate to contact us for more information.
References
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Rillahan, C. D., et al.Glycan microarrays for decoding the glycome. Annual review of biochemistry. 2011, 80: 797–823.
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Raman, R.; et al. Glycomics: an integrated systems approach to structure-function relationships of glycans. Nature methods. 2005, 2(11):817-24.
For Research Use Only.
Related Services:
- Glycan Profiling of Various Glycoprotein
- Glycan Labeling
- Technologies for Glycan Profiling
- Use Glycoenzymes to Understand Glycan Structure and Function
- Visualize Terminal Glycans Using Fluorescence or SDS-PAGE
- Glycans in Immunity
