Article
A point mutation uncouples human interleukin-1 beta biological activity and receptor binding.
The Journal of biological chemistry - 15 Apr 1990
Gehrke L, Jobling S A, Paik L S, McDonald B, Rosenwasser L J, Auron P E
Abstract excerpt
Interleukin-1 proteins elicit a number of biological activities, but the molecular events following formation of a cell surface receptor-ligand complex have not been well defined. Conversion of Arg127 to Gly127 in the mature human interleukin-1 beta protein reduces bioactivity by 100-fold while the receptor binding affinity decreases by only 25%. The results suggest that the mutant IL-1 beta protein is defective...
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