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Related Concept Videos

Glycosaminoglycans01:23

Glycosaminoglycans

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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.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
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Proteoglycans01:05

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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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Protein Networks02:26

Protein Networks

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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.
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
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Protein Glycosylation01:25

Protein Glycosylation

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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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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

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Glycosaminoglycan interaction networks and databases.

Sylvie Ricard-Blum1, Serge Perez2

  • 1Univ. Lyon, Université Lyon 1, ICBMS, UMR 5246, 69622 Villeurbanne, France.

Current Opinion in Structural Biology
|March 20, 2022
PubMed
Summary
This summary is machine-generated.

Glycosaminoglycans (GAGs) are diverse polysaccharides crucial for cell interactions and signaling. New methods identify GAG-protein interactions, revealing biological mechanisms and potential therapeutic targets.

Keywords:
DatabasesGlycosaminoglycansInteractionsNetworksStructure

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Glycobiology

Background:

  • Glycosaminoglycans (GAGs) are structurally diverse polysaccharides essential for the extracellular matrix, cell-matrix interactions, and cell signaling.
  • Understanding GAG functions requires characterizing their interactions with proteins.

Purpose of the Study:

  • To explore methods for identifying and characterizing glycosaminoglycan-protein interactions.
  • To leverage these interactions to understand GAG functions and develop therapeutic strategies.

Main Methods:

  • Utilizing microarray technology to screen natural and synthetic GAG libraries for protein binding partners.
  • Employing advanced GAG sequencing techniques to identify specific GAG sequences involved in protein binding.
  • Applying GAG-mediated pull-down proteomics to identify GAG-binding proteins across proteomes.

Main Results:

  • Identification of specific GAG sequences and structural features that mediate protein binding.
  • Construction of GAG interaction networks (interactomes) based on experimental data.
  • Discovery of novel GAG-binding proteins and elucidation of their roles in biological processes.

Conclusions:

  • Advanced techniques enable comprehensive characterization of GAG-protein interactions.
  • GAG interactomes provide insights into molecular mechanisms and cellular functions.
  • These findings support the development of targeted inhibitors for therapeutic applications.