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 t...
Topics
- Amino Acid Sequence
- Arginine
- DNA Replication
- Enzyme-Linked Immunosorbent Assay
- Glycine
- Humans
- Interleukin-1
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Plasmids
- Protein Biosynthesis
- Protein Conformation
- Radioligand Assay
- Receptors, Immunologic
- Receptors, Interleukin-1
- T-Lymphocytes, Helper-Inducer