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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Oligosaccharide Assembly01:24

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Proteoglycans01:05

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
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The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Supplementing the Carbohydrate Structure Database with glycoepitopes.

Philip V Toukach1

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This study links carbohydrate structures with immune epitopes, enabling exploration of shared glycan structures across organisms. Database integration reveals valuable taxonomic and medical data.

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Area of Science:

  • Immunology
  • Glycomics
  • Bioinformatics

Background:

  • The Immune Epitope Database (IEDB) contains extensive immunological data.
  • The Carbohydrate Structure Database (CSDB) houses detailed information on carbohydrate structures.
  • Integrating these databases can enhance biological data exploration.

Purpose of the Study:

  • To map carbohydrate structures from CSDB to glycoepitopes in IEDB.
  • To enable users to explore shared glycan structures and their associated epitopes across different organisms.
  • To demonstrate the benefits of integrating immunological and glycomic databases.

Main Methods:

  • Referencing carbohydrate structures in CSDB to glycoepitopes in IEDB.
  • Developing a mapping system to link structural determinants.
  • Retrieving associated taxonomic, medical, and other data for shared glycans.

Main Results:

  • Successful referencing of CSDB carbohydrate structures to IEDB glycoepitopes.
  • Identification of shared glycan structures across various organisms based on epitopes.
  • Facilitation of access to associated taxonomic and medical data for these shared glycans.

Conclusions:

  • The integration of immunological and glycomic databases provides significant advantages.
  • This mapping allows for a deeper understanding of glycan structures and their immunological relevance.
  • Users can explore cross-species glycan similarities and associated biological information.