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Related Concept Videos

Proteoglycans01:05

Proteoglycans

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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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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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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.
Glycosylation occurs in...
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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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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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.
Multiple sugar molecules that may or may...
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Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining
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Demystifying heparan sulfate-protein interactions.

Ding Xu1, Jeffrey D Esko

  • 1Department of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, California 92093; email: dxu@ucsd.edu , jesko@ucsd.edu.

Annual Review of Biochemistry
|March 11, 2014
PubMed
Summary

Many proteins traditionally called heparin-binding proteins actually bind heparan sulfate chains on cell surfaces. This review clarifies these heparan sulfate-binding proteins (HSBPs) and their interactions, enhancing understanding of heparan sulfate

Keywords:
glycan–protein interactionglycosaminoglycanheparan sulfate–binding domainheparin-binding proteinoligomerizationproteoglycan

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Glycobiology

Background:

  • Numerous proteins, including cytokines, enzymes, and receptors, bind heparin.
  • Traditionally classified as heparin-binding proteins, their physiological interactions differ.

Purpose of the Study:

  • To reclassify heparin-binding proteins as heparan sulfate-binding proteins (HSBPs).
  • To review the interaction modes between heparan sulfate and HSBPs.
  • To emphasize biochemical and structural insights into these interactions.

Main Methods:

  • Literature review focusing on biochemical and structural data.
  • Analysis of protein-proteoglycan interactions.
  • Classification of proteins based on binding specificities.

Main Results:

  • Proteins primarily interact with heparan sulfate chains of proteoglycans, not free heparin.
  • Heparan sulfate-binding proteins (HSBPs) represent a more accurate classification.
  • Diverse interaction modes exist between heparan sulfate and HSBPs.

Conclusions:

  • Heparan sulfate-binding proteins (HSBPs) are crucial for various biological functions.
  • Understanding these interactions provides key insights into heparan sulfate's roles.
  • Biochemical and structural studies are vital for elucidating HSBPs' functions.