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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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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 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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Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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The current structural glycome landscape and emerging technologies.

Liviu Copoiu1, Sony Malhotra2

  • 1Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, United Kingdom.

Current Opinion in Structural Biology
|February 2, 2020
PubMed
Summary
This summary is machine-generated.

Researchers face challenges in understanding the complex "glycocode." This review explores strategies and tools, including the Protein Data Bank (PDB), to advance glycobiology research and glycan structure determination.

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Area of Science:

  • Glycobiology
  • Structural Biology
  • Molecular Biology

Background:

  • Carbohydrates (glycans) are fundamental biomolecules involved in critical cellular processes.
  • Despite their importance, the 'glycocode' remains largely undeciphered.
  • Challenges persist in understanding glycan structure and function.

Purpose of the Study:

  • To review challenges in glycobiology research.
  • To present strategies for overcoming these challenges.
  • To provide a comprehensive overview of the current saccharide landscape in the Protein Data Bank (PDB).

Main Methods:

  • Review of existing literature and databases (e.g., PDB).
  • Analysis of software development impact on carbohydrate structure determination.
  • Examination of molecular and cellular biology techniques for glycan analysis.

Main Results:

  • Identification of key challenges in structural and functional glycan research.
  • Highlighting the utility of the PDB for studying carbohydrate structures.
  • Discussion of advancements in computational and experimental methodologies.

Conclusions:

  • Overcoming current challenges requires integrated strategies.
  • Continued development of tools and methods is crucial for deciphering the glycocode.
  • Enhanced understanding of glycans will impact various fields from medicine to materials science.