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Role of leucine residues in the C‐terminal region of human interleukin‐6 in the biological activity
Author(s) -
Nishimura Chiaki,
Ekida Teiji,
Nomura Kazuhide,
Sakamoto Koji,
Suzuki Hiroshi,
Yasukawa Kiyoshi,
Kishimoto Tadamitsu,
Arata Yoji
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81118-6
Subject(s) - leucine , terminal (telecommunication) , chemistry , biochemistry , amino acid , computer science , telecommunications
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 Leu 168,175,182 →Val were only 1% compared with those of wild‐type IL‐6. However, the mutant Leu 152,159,166 →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 Leu 168 ‐Met 185 , but not for the peptide Leu 152 ‐Arg 169 . These results indicate that leucine residues in the C‐terminal region, especially Leu 168 , Leu 175 , and Leu 182 , play an important role in the receptor‐binding and Ig‐induction activities.