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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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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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Functional groups are groups of atoms with specific chemical properties that occur within organic molecules and are sometimes denoted as “R”. Functional groups can “functionalize” a compound by enabling it to adopt different physical and chemical properties.
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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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O-GlcNAc informatics: advances and trends.

Chunyan Hou1, Weiyu Li1,2, Yaoxiang Li1

  • 1Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, Washington, DC, 20007, USA.

Analytical and Bioanalytical Chemistry
|September 18, 2024
PubMed
Summary

This review surveys bioinformatics tools for O-Linked β-N-acetylglucosamine (O-GlcNAc) modification research. These informatics resources aid in analyzing O-GlcNAc proteomics data and identifying modification sites.

Keywords:
DatabasesGlycoinformaticsO-GlcNAcO-GlcNAc proteomicsO-GlcNAcylationOGT

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Area of Science:

  • Biochemistry and Molecular Biology
  • Bioinformatics and Computational Biology

Background:

  • Protein glycosylation, specifically O-Linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation), is a critical post-translational modification involved in numerous cellular processes and diseases.
  • The significance of O-GlcNAcylation has gained increasing recognition, driving the development of specialized bioinformatics tools.

Purpose of the Study:

  • To provide a comprehensive review of O-GlcNAc informatics tools developed over the past four decades.
  • To catalog software, databases, and servers relevant to O-GlcNAc research, facilitating data analysis, site prediction, and enzyme interaction studies.

Main Methods:

  • Literature review and survey of existing O-GlcNAc-focused bioinformatics software and databases.
  • Categorization of tools based on their application in O-GlcNAc proteomics data analysis, experimentally identified sites, prediction of O-GlcNAc sites, and enzyme interaction studies.

Main Results:

  • Identification and description of various bioinformatics tools and databases supporting O-GlcNAc research.
  • Highlighting resources for analyzing O-GlcNAc proteomics data, accessing experimentally validated O-GlcNAc sites, predicting novel modification sites, and exploring interactions with O-GlcNAc cycling enzymes.

Conclusions:

  • O-GlcNAc informatics tools have significantly advanced O-GlcNAcylation research, offering unique perspectives on protein modification.
  • This review serves as a valuable resource for researchers and aims to stimulate the development of more sophisticated informatic tools for future O-GlcNAc studies.