Article
Variations in the unstructured C-terminal tail of interferons contribute to differential receptor binding and biological activity.
Journal of molecular biology - 28 Jul 2006
Slutzki Michal, Jaitin Diego A, Yehezkel Tuval Ben, Schreiber Gideon
Abstract excerpt
Type I interferons (IFNs) elicit antiviral, antiproliferative and immunomodulatory properties in cells. All of them bind to the same receptor proteins, IFNAR1 and IFNAR2, with different affinities. While the 13 known IFNalphas are highly conserved, the C-terminal unstructured tail was found to have large variation in its net charge, from neutral to +4. This led us to speculate that the tail may have a role in...
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