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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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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.
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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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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Phenylketonuria (PKU) is a protein metabolism disorder characterized by high blood levels of the amino acid phenylalanine. This results from a mutation in the gene responsible for phenylalanine hydroxylase, an enzyme that converts phenylalanine into tyrosine. When this enzyme is deficient, phenylalanine builds up in the blood, leading to symptoms such as vomiting, rashes, seizures, growth deficiency, and severe mental retardation. An early diagnosis and a diet restricting phenylalanine intake...
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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Updated: Sep 16, 2025

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
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Are N-linked glycans intrinsically disordered?

Eliza Gazaway1, Rajan Kandel1, Oliver C Grant1

  • 1Complex Carbohydrate Research Center and Department of Biochemistry and Molecular Biology, University of Georgia, 315 Riverbend Road, Athens, 30602, Georgia.

Current Opinion in Structural Biology
|July 11, 2025
PubMed
Summary
This summary is machine-generated.

N-linked glycosylation is crucial for protein function but challenging to study structurally. This work explores the dynamic properties of N-linked glycans and the limitations of current research methods.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • N-linked glycosylation is a vital protein modification affecting stability and function.
  • Experimental 3D structures of N-linked glycans are rare due to flexibility and heterogeneity.
  • Computational modeling is essential for understanding glycoprotein structures.

Purpose of the Study:

  • To review the dynamic properties of N-linked glycans.
  • To focus on glycan presentation and orientation on protein surfaces.
  • To discuss limitations in experimental and theoretical glycoprotein studies.

Main Methods:

  • Review of current literature on N-linked glycan dynamics.
  • Analysis of factors influencing glycan presentation.
  • Discussion of experimental and computational modeling limitations.

Main Results:

  • N-linked glycans exhibit dynamic properties impacting their presentation.
  • Significant limitations exist in experimental validation of computational models.
  • The intrinsic disorder of N-linked glycans is questioned.

Conclusions:

  • Understanding N-linked glycan dynamics is critical for glycoprotein research.
  • Further development of experimental and computational methods is needed.
  • The dynamic and potentially disordered nature of N-linked glycans requires further investigation.