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Protein Glycosylation

Protein Glycosylation

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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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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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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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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Updated: Jan 8, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

GlyContact analyzes glycan 3D structures at scale.

Luc Thomès¹, Roman Joeres^2,3,4, Zeynep Akdeniz^2,3

¹University Lille, CHU Lille, ULR 7364 - RADEME - Maladies RAres du DÉveloppement embryonnaire et du Métabolisme, Lille, France.

Nature Communications

|December 12, 2025

Summary

This summary is machine-generated.

GlyContact is a new Python package for analyzing 3D glycan structures. It helps understand how glycan structure impacts function and improves predictions of lectin-glycan binding.

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Area of Science:

Carbohydrate chemistry and structural biology.
Computational glycobiology and bioinformatics.

Background:

Glycans are complex biomolecules with challenging structural characterization, hindering the understanding of their structure-function relationships.
Existing databases like GlycoShape offer 3D glycan structures from simulations, but tools for their analysis are needed.

Purpose of the Study:

To introduce GlyContact, an open-source Python package for retrieving, processing, and analyzing 3D glycan structures.
To demonstrate GlyContact's utility in exploring glycan structural dynamics and their impact on biological interactions.

Main Methods:

Development of the GlyContact Python package for glycan structure analysis.
Utilizing molecular dynamics (MD) simulations, NMR, and X-ray crystallography data.
Application of von Mises graph neural networks for predicting disaccharide torsion angle distributions.

Main Results:

GlyContact reveals the influence of sequence context on glycan motif structure.
The package provides insights into glycan flexibility and surface accessibility, improving lectin-binding prediction by approximately 7%.
Accurate prediction of torsion angle distributions between disaccharides was achieved.

Conclusions:

GlyContact facilitates the exploration of 3D glycan structures, offering valuable insights into their biological functions.
The tool enhances the understanding of glycan-lectin interactions and structural dynamics.
GlyContact is an open-access resource empowering researchers in glycobiology.