ArticleJournal of molecular modeling2019
Molecular modeling of the effects of glycosylation on the structure and dynamics of human interferon-gamma.
Article in Journal of molecular modeling, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- The Role of Glycan Structures in Modulating GM-CSF Bioactivity: Insights from Glycoengineering.bioRxiv : the preprint server for biology · 2026Article
- Theoretical Study of the Influence of K20N Glycosylation on the Dynamic Behavior of Im7 Protein.Molecules (Basel, Switzerland) · 2025Article
- Implications of glycosylation for the development of selected cytokines and their derivatives for medical use.Biotechnology advances · 2024Review
- Molecular analysis of the type III interferon complex and its applications in protein engineering.Biophysical journal · 2023Article
- Scalable production of tissue-like vascularized liver organoids from human PSCs.Experimental & molecular medicine · 2023Article
- Heparan Sulfate Facilitates Binding of hIFNInternational journal of molecular sciences · 2022Article
- Complement Factor H in cSCC: Evidence of a Link Between Sun Exposure and Immunosuppression in Skin Cancer Progression.Frontiers in oncology · 2022Article
- Molecular Mechanism of the Anti-Inflammatory Action of Heparin.International journal of molecular sciences · 2021Article
- Proteomic and molecular dynamic investigations of PTM-induced structural fluctuations in breast and ovarian cancer.Scientific reports · 2021Observational
- Article
- Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein.International journal of molecular sciences · 2020Review
- The role of interferon-γ in cardiovascular disease: an update.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2020Review
- Roles of IFN-γ in tumor progression and regression: a review.Biomarker research · 2020Review
- Transient Co-Expression of Bioactive Murine Interferon-Gamma and HBsAg in Tobacco and Lettuce Leaves.Avicenna journal of medical biotechnologyArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Natural hIFNγ is a glycoprotein with two N-glycosylation sites in each monomer chain, which are independently and differentially glycosylated. Although glycosylation is not necessary for the activity of the cytokine, it was proposed that it protects the cytokine from proteolytic degradation and thus extends its circulatory half-life. Here, we report the development of model structures of glycosylated full-length native hIFNγ homodimers. Our aim is to shed light on the mechanism through which glycosylation preserves the integrity of the cytokine molecule. To this end, we employ molecular dynamics simulations to study the interaction of the carbohydrate chains with the receptor-binding sites in the cytokine and with its flexible highly positively charged C-termini. The glycans interact primarily with the globular part of the protein, but also occasionally form contacts with the solvent-exposed and sensitive to proteases C-terminal tails. We show that the glycans restrict the C-termini wagging motion into the solvent, limit their flexibility and keep them closer to the α-helical globule of hIFNγ, thus possibly protecting them from proteolytic processing.
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Registered trials
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