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Related Concept Videos

Glycosaminoglycans01:23

Glycosaminoglycans

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...
Proteoglycans01:05

Proteoglycans

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,...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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...
Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
Factors Affecting Protein-Drug Binding: Drug Interactions01:23

Factors Affecting Protein-Drug Binding: Drug Interactions

Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...

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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Serpin-glycosaminoglycan interactions.

Chantelle M Rein1, Umesh R Desai, Frank C Church

  • 1Department of Pathology and Laboratory Medicine, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.

Methods in Enzymology
|November 15, 2011
PubMed
Summary

Certain serine protease inhibitors (serpins) use glycosaminoglycans (GAGs) as cofactors to significantly enhance protease inhibition rates. This study focuses on three key GAG-binding serpins involved in coagulation: antithrombin, heparin cofactor II, and protein C inhibitor.

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Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining
05:57

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Published on: February 25, 2021

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Serpins are traditionally classified by structural homology, but cofactor requirements for protease inhibition vary.
  • Some serpins, including antithrombin (AT), heparin cofactor II (HCII), and protein C inhibitor (PCI), require glycosaminoglycans (GAGs) for maximal protease inhibition.
  • GAGs like heparin, heparan sulfate, and dermatan sulfate act as essential cofactors for specific GAG-binding serpins.

Purpose of the Study:

  • To explore the role of GAGs as cofactors for serine protease inhibitors (serpins).
  • To discuss the structural basis of serpin-GAG interactions, focusing on conserved binding regions.
  • To review methodologies for studying serpin-GAG interactions and the physiological roles of key GAG-binding serpins in coagulation.

Main Methods:

  • Structural analysis of serpins and their interaction sites with GAGs.
  • Investigation of conformational changes induced by GAG binding.
  • Utilizing mouse models to study the biological functions of GAG-binding serpins in vivo.

Main Results:

  • GAG binding to serpins, typically near helix D (except PCI at helix H), can induce conformational changes.
  • These conformational changes enhance protease binding and accelerate inhibition rates by up to 10,000-fold.
  • AT, HCII, and PCI are key GAG-binding serpins modulating coagulation, with distinct GAG cofactor preferences.

Conclusions:

  • GAGs are critical cofactors for a subset of serpins, significantly impacting their inhibitory function.
  • Understanding serpin-GAG interactions is crucial for elucidating their roles in physiological processes like coagulation.
  • Further research utilizing advanced techniques and animal models will deepen our knowledge of these vital molecular interactions.