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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
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Key regulators of galectin-glycan interactions
Nourine A Kamili1, Connie M Arthur1, Christian Gerner-Smidt1
1Center for Transfusion Medicine and Cellular Therapies, Department of Laboratory Medicine and Pathology, Emory University School of Medicine, Atlanta, GA, USA.
Proteomics
|September 2, 2016
Summary
Glycan binding proteins (GBPs) mediate crucial biological processes. This review explores how modifying glycans impacts galectin-glycan interactions and their regulatory roles.
Area of Science:
- Biochemistry
- Molecular Biology
- Glycobiology
Background:
- Protein-ligand interactions are vital for biological regulation.
- Glycan binding proteins (GBPs) and their glycan targets are key players.
- Cell surface and secreted proteins are often glycosylated, influencing interactions.
Purpose of the Study:
- To review factors affecting galectin activity.
- To examine the impact of glycan modifications on galectin-glycan interactions.
Main Methods:
- Literature review of galectin-glycan interactions.
- Analysis of glycan structure and modification effects.
Main Results:
- Galectins bind diverse glycan structures.
- Glycan modifications significantly alter galectin recognition and function.
- Altered glycosylation impacts biological processes regulated by galectins.
Conclusions:
- Galectin activity is modulated by glycan determinants.
- Understanding these interactions is crucial for deciphering biological regulation.
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