Nishimura C, Ekida T, Nomura K, Sakamoto K, Suzuki H, Yasukawa K, Kishimoto T, Arata Y
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
FEBS Lett. 1992 Oct 26;311(3):271-5. doi: 10.1016/0014-5793(92)81118-6.
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.
对人白细胞介素-6（IL-6）C端区域每隔七个位置出现的两组三个周期性亮氨酸残基进行了定点诱变。三重突变体Leu168,175,182→Val的受体结合活性和免疫球蛋白（Ig）诱导活性与野生型IL-6相比仅为1%。然而，突变体Leu152,159,166→Val具有野生型IL-6的13%的受体结合活性和2%的Ig诱导活性。为了获得关于受体结合区域更直接的信息，我们制备了两种合成肽。观察到肽Leu168-Met185具有显著的结合活性，而肽Leu152-Arg169则没有。这些结果表明，C端区域的亮氨酸残基，尤其是Leu168、Leu175和Leu182，在受体结合和Ig诱导活性中起重要作用。
