FEBS Letters | |
Role of leucine residues in the C‐terminal region of human interleukin‐6 in the biological activity | |
Ekida, Teiji2  Nomura, Kazuhide2  Sakamoto, Koji2  Kishimoto, Tadamitsu1  Nishimura, Chiaki2  Arata, Yoji2  Suzuki, Hiroshi3  Yasukawa, Kiyoshi3  | |
[1] Department of Medicine III, Osaka University Medical School, Fukushima-ku, Osaka, Japan;Faculty of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo, Japan;Tosoh Corporation, Ayase-shi, Kanagawa, Japan | |
关键词: Interleukin 6; Site-directed mutagenesis; Peptide fragment; Receptor-binding activity; B-Cell stimulatory activity; Human; IL-6; interleukin-6; E. coli; Escherichia coli; Ig; immunoglobulin; hGH; human growth hormone; ELISA; enzyme-linked immunosorbent assay; | |
DOI : 10.1016/0014-5793(92)81118-6 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Site-directed mutagenesis of two sets of three periodic leucine residues which appear at every seventh position in the C-terminal region of human interleukin-6 (IL-6) was performed. Both receptor-binding and immunoglobulin (Ig)-induction activities of a triple mutant Leu168,175,182→Val were only 1% compared with those of wild-type IL-6. However, the mutant Leu152,159,166→Val had 13% receptor-binding and 2% Ig-induction activities of those of wild-type IL-6. In order to obtain more direct information on the receptor-binding region, we prepared two synthetic peptides. A significant binding activity was observed for the peptide Leu168-Met185, but not for the peptide Leu152-Arg169. These results indicate that leucine residues in the C-terminal region, especially Leu168, Leu175, and Leu182, play an important role in the receptor-binding and Ig-induction activities.
【 授权许可】
Unknown
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