Interleukin 1 receptor antagonist is a member of the interleukin 1 gene family: evolution of a cytokine control mechanism
| Autor: | P Heimdal, Robert C. Thompson, M T Brewer, Stephen P. Eisenberg, Barbara J. Brandhuber, E Verderber |
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| Rok vydání: | 1991 |
| Předmět: |
Molecular Sequence Data
Interleukin 5 receptor alpha subunit Retinoic acid receptor beta Biology Interleukin 10 receptor alpha subunit Mice Interleukin 26 Sequence Homology Nucleic Acid Animals Humans Amino Acid Sequence Receptors Immunologic Interleukin 12 receptor beta 1 subunit G alpha subunit Genetics Multidisciplinary Base Sequence Receptors Interleukin-1 Rats Inbred Strains TGF beta receptor 2 Introns Rats Multigene Family Mutation Interleukin 1 receptor type I Sequence Alignment Research Article Interleukin-1 |
| Zdroj: | Proceedings of the National Academy of Sciences. 88:5232-5236 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.88.12.5232 |
| Popis: | Interleukin 1 receptor antagonist (IL-1ra) is a protein that binds to the IL-1 receptor and blocks the binding of both IL-1 alpha and -beta without inducing a signal of its own. Human IL-1ra has some sequence identity to human IL-1 beta, but the evolutionary relationship between these proteins has been unclear. We show that the genes for human, mouse, and rat IL-1ra are similar to the genes for IL-1 alpha and IL-1 beta in intron-exon organization, indicating that gene duplication events were important in the creation of this gene family. Furthermore, an analysis of sequence comparisons and mutation rates for IL-1 alpha, IL-1 beta, and IL-1ra suggests that the duplication giving rise to the IL-1ra gene was an early event in the evolution of the gene family. Comparisons between the mature sequences for IL-1ra, IL-1 alpha, and IL-1 beta suggest that IL-1ra has a beta-stranded structure like to IL-1 alpha and IL-1 beta, consistent with the three proteins being related. The N-terminal sequences of IL-1ra appear to be derived from a region of the genome different than those of IL-1 alpha and IL-1 beta, thus explaining their different modes of biosynthesis and suggesting an explanation for their different biological activities. |
| Databáze: | OpenAIRE |
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