# Interferon‐γ binds to heparan sulfate by a cluster of amino acids located in the C‐terminal part of the molecule

@article{LortatJacob1991InterferonBT,
title={Interferon‐$\gamma$ binds to heparan sulfate by a cluster of amino acids located in the C‐terminal part of the molecule},
author={Hugues Lortat-Jacob and Jean Alexis Grimaud},
journal={FEBS Letters},
year={1991},
volume={280}
}
• Published 11 March 1991
• Biology, Chemistry
• FEBS Letters
77 Citations
• Biology, Chemistry
Journal of the American Chemical Society
• 2013
The binding mechanism described herein, by which the D2 domain kinetically drives the interaction, has important functional consequences and gives a structural framework to better understand how specific are the interactions between proteins and heparin.
• Biology
Cytokine
• 1999
Analysis of the ability of Glycosaminoglycans to interact with human interferon gamma and the effect of those interactions on its biologic activity suggests important regulatory roles for GAGs on the activity of IFN-gamma in vivo.
• Biology
Cytokine
• 2000
It is suggested that heparin and chondroitin sulfate modulate IFN-gamma activity by causing structural changes in the IFN -gamma dimer.
• Biology
The Biochemical journal
• 2004
Evidence is provided of a binding through electrostatic interactions between the charged side chains of the protein and the sulphate groups of heparin that does not induce specific conformation of the C-terminal part of IFNgamma.
• Biology, Medicine
The Journal of Biological Chemistry
• 1996
The data demonstrate that the blood clearance of the cytokine is a non-receptor-mediated process and that in vivo the local concentration of heparan sulfate/heparin-like molecules regulates IFN-γ activity by a unique mechanism involving a controlled processing of its carboxyl-terminal sequence.
• Biology
The Journal of Biological Chemistry
• 1998
It is found that IFNγ bound to heparin displayed a strongly reduced affinity for its receptor, which is consistent with the fact that a cluster of basic amino acids in the carboxyl-terminal sequence of the cytokine was involved both inheparin and receptor recognition.
• Biology, Medicine
European journal of immunology
• 1995
This study analyzes the effect of heparin and heparan sulfate on three different IFN‐γ‐mediated activities inducible in human glioblastoma cells.

## References

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Journal of immunology
• 1987
The results suggest that the carboxyl terminus of human IFN-gamma contributes significantly to the formation of the receptor-binding site of the molecule.
• Biology
Protein engineering
• 1990
The results suggest that most residues within the cassette can be altered without significant effects on biological activity, and confirm earlier observations of the important role of basic residues in the 128-131 region of the molecule for biological activity.