| First Author | Thomassen E | Year | 1999 |
| Journal | Cytokine | Volume | 11 |
| Issue | 6 | Pages | 389-99 |
| PubMed ID | 10346978 | Mgi Jnum | J:55824 |
| Mgi Id | MGI:1339443 | Doi | 10.1006/cyto.1998.0452 |
| Citation | Thomassen E, et al. (1999) Identification and characterization of SIGIRR, a molecule representing a novel subtype of the IL-1R superfamily. Cytokine 11(6):389-99 |
| abstractText | A novel member of the interleukin 1 receptor (IL-1R) superfamily, SIGIRR (single Ig IL-1R-related molecule) was identified in mouse and human. Although it shows the typical conserved motifs that characterize the IL-1R and Toll superfamily, it is structurally and functionally distinct from both. SIGIRR has only one Ig domain in its extracellular portion whereas the IL-1R family contains three Ig folds, An unusually long cytoplasmic domain is reminiscent of the structure of drosophila Toll, yet the SIGIRR peptide sequence is more closely related to IL-1RI. The human SIGIRR gene maps to 11p15.5 and thus is not located in the same cluster on chromosome 2 that is known to contain four members of the IL-1R family. It failed to bind to the known IL-1-family members and, when co- expressed with the IL-1RI, had no effect on the binding of IL-1 and on subsequent nuclear factor kappa B (NF kappa B) activation, A chimera, in which the SIGIRR intracellular domain was fused to the IL-1R extracellular domain, did not activate NF kappa B unlike similar fusion proteins of other IL-1R related molecules. We conclude that the SIGIRR protein represents a novel subtype of the IL-1R superfamily, (C) 1999 Academic Press. |
