Related Experiment Video
Updated: Sep 21, 2025
11:21
Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
3.6K
Reading the glyco-code: New approaches to studying protein-carbohydrate interactions
Simon Wisnovsky1, Carolyn R Bertozzi2
1Faculty of Pharmaceutical Sciences, University of British Columbia, Vancouver, BC, V6T 1Z3, Canada.
Current Opinion in Structural Biology
|June 2, 2022
Summary
Identifying ligands for glycan-binding proteins (GBPs) is crucial for understanding cell function. Recent advances in cell-based glycan arrays and glyco-genomic profiling offer precise methods for studying these interactions in living cells.
Area of Science:
- Glycoscience
- Molecular Biology
- Cell Biology
Background:
- Cell surfaces feature carbohydrate molecules (glycans) that bind to hundreds of functional proteins.
- Glycan-protein binding events significantly influence protein and cell functions.
- Identifying specific ligands for glycan-binding proteins (GBPs) remains a key challenge in glycoscience.
Purpose of the Study:
- To review recent advancements in precisely dissecting protein-carbohydrate interactions.
- To highlight novel methods for defining the structural determinants of glycan-protein interactions.
- To explore new opportunities for studying glycans in physiological and disease contexts.
Main Methods:
- Cell-based glycan arrays for high-throughput screening.
- Glyco-genomic profiling for comprehensive analysis.
- Advanced techniques for precise dissection of molecular interactions.
Main Results:
- Demonstrated unprecedented precision in analyzing protein-carbohydrate interactions.
- Detailed the structural determinants of glycan-protein binding within living cells.
- Showcased the utility of novel methods in glycoscience research.
Conclusions:
- Cell-based glycan arrays and glyco-genomic profiling are powerful tools for understanding glycan-protein interactions.
- These methods provide new avenues for investigating the role of glycans in health and disease.
- Future research can leverage these techniques to advance glycoscience and its clinical applications.
More Related Videos
Related Concept Videos
01:25Protein Glycosylation
7.4K
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.
Glycosylation occurs in...
Glycosylation occurs in...
7.4K
02:04Protein-protein Interfaces
13.8K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
13.8K
02:26Protein Networks
4.1K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.1K
01:24Oligosaccharide Assembly
3.0K
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.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
3.0K
02:35Noncovalent Attractions in Biomolecules
56.0K
Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
56.0K
01:24Protein Organization
7.3K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
The primary structure of a protein is its amino acid sequence....
7.3K