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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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...
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
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,...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

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Related Experiment Video

Updated: Jun 8, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Glycosylation stabilizes TNFα and receptor complexes: structural and biophysical implications.

Karolina Sławińska1, Gabriela Całka-Kuc1, Martyna Maszota-Zieleniak2

  • 1Department of Biomedical Chemistry, Faculty of Chemistry, University of Gdańsk, Wita Stwosza 63, Gdańsk, 80-308, Poland.

Carbohydrate Research
|June 6, 2026
PubMed
Summary

Glycosylation enhances tumor necrosis factor alpha (TNFα) binding to its receptors TNFR1 and TNFR2. This modification increases protein stability and receptor interaction affinity, impacting cytokine signaling pathways.

Keywords:
GlycosylationMicroscale thermophoresisMolecular dynamicsProtein stabilityTNFR1TNFR2TNFαnanoDSF

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Related Experiment Videos

Last Updated: Jun 8, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Immunology

Background:

  • Glycosylation is a key post-translational modification influencing protein function.
  • The precise impact of glycosylation on cytokine-receptor interactions, specifically TNFα with TNFR1 and TNFR2, requires further elucidation.

Purpose of the Study:

  • To investigate the mechanistic effects of TNFα glycosylation on its binding affinity and stability with TNFR1 and TNFR2.
  • To elucidate the role of glycan structures in mediating TNFα-receptor complex formation and stability.

Main Methods:

  • Utilized biophysical techniques including nano differential scanning fluorescence (nanoDSF) for thermal stability assessment and microscale thermophoresis (MST) for binding affinity quantification.
  • Employed molecular modeling and molecular dynamics (MD) simulations to analyze the structural and energetic contributions of glycosylation to TNFα-receptor complexes.

Main Results:

  • Glycosylated TNFα demonstrated enhanced thermal stability and formed more stable complexes with TNFR1 and TNFR2 compared to non-glycosylated TNFα.
  • Significant increases in binding affinity were observed for glycosylated TNFα with TNFR2 (four-fold increase) and TNFR1 (detectable binding vs. undetectable for non-glycosylated).
  • MD simulations revealed that glycans favorably contribute to complex stability, with effects varying by glycan length and receptor type, particularly pronounced for TNFR1.

Conclusions:

  • TNFα glycosylation promotes the formation of more stable receptor complexes and enhances binding affinity through glycan-mediated stabilization effects.
  • These findings provide a qualitative model for understanding how glycosylation modulates cytokine-receptor interactions and signaling outcomes.