Internal deletions of amino acids 29-42 of human interleukin-6 (IL-6) differentially affect bioactivity and folding.
Internal deletions of the human interleukin-6 (IL-6) cDNA have been generated in the region encoding residues 29 to 42. Mutant proteins were produced by in vitro transcription-translation or in Escherichia coli and tested for their biological activity using the hybridoma growth factor (HGF) assay or a transcriptional activation assay on human hepatoma cells. The folding of the mutants was also checked by immunoprecipitation with conformation-specific monoclonal antibodies. The results show that only residues 29 to 34 are crucial for IL-6 activity and that the first two amino acids are probably involved in the definition of the IL-6 active site.
Arcone
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CEINGE, Centro di Ingegneria Genetica, Napoli, Italy.
Fontaine
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Coto
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Brakenhoff
J P
JP
Content
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Ciliberto
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G
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D015850:Interleukin-6 / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D010446:Peptide Fragments; D011233:Precipitin Tests; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000096:biosynthesis; D014407:Tumor Cells, Cultured
D000911:Antibodies, Monoclonal; D015850:Interleukin-6; D010446:Peptide Fragments; D011994:Recombinant Proteins