Role of leucine residues in the C-terminal region of human interleukin-6 in the biological activity
| Autor: | Kazuhide Nomura, Koji Sakamoto, Hiroshi Suzuki, Kiyoshi Yasukawa, Tadamitsu Kishimoto, Teiji Ekida, Yoji Arata, Chiaki Nishimura |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Herpesvirus 4
Human Leucine zipper Molecular Sequence Data Mutant Biophysics Peptide Interleukin 6 Binding Competitive Biochemistry Structure-Activity Relationship Leucine Structural Biology Escherichia coli Genetics Humans Amino Acid Sequence Cloning Molecular Receptors Immunologic Site-directed mutagenesis Molecular Biology Cell Line Transformed chemistry.chemical_classification B-Lymphocytes Base Sequence biology Interleukin-6 Mutagenesis Receptor-binding activity B-Cell stimulatory activity Peptide fragment Biological activity Cell Biology Receptors Interleukin-6 Molecular biology Peptide Fragments Recombinant Proteins Oligodeoxyribonucleotides chemistry Antibody Formation Mutagenesis Site-Directed biology.protein Antibody Human |
| Zdroj: | FEBS Letters. (3):271-275 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(92)81118-6 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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