Mutated interleukin-5 monomers are biologically inactive.

Abstract excerpt

Interleukin-5 contains only two cysteine residues both of which appear to be involved in the dimerisation of the molecule to form a disulphide-linked homodimer (Minamitake et al., J. Biochem. 107, 292-297, 1990). However, it remains unclear whether this linkage is necessary for the bioactivity of this cytokine. Site-directed mutagenesis was used to produce amino acid substitutions of either or both of the...

Topics

• Animals
• Cells, Cultured
• Cysteine
• In Vitro Techniques
• Interleukin-5
• Macromolecular Substances
• Mice
• Molecular Structure
• Mutation
• Receptors, Immunologic
• Receptors, Interleukin
• Receptors, Interleukin-5