Structural highlights
Function
[IL1R1_HUMAN] Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the corecptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex.[1]
Publication Abstract from PubMed
Interleukin-1 (IL-1)-family cytokines are mediators of innate and adaptive immunity. They exert proinflammatory effects by binding a primary receptor that recruits a receptor accessory protein to form a signaling-competent heterotrimeric complex. Here we present the crystal structure of IL-1beta bound to its primary receptor IL-1RI and its receptor accessory protein IL-1RAcP, providing insight into how IL-1-type cytokines initiate signaling and revealing an evolutionary relationship with the fibroblast growth factor receptor family.
Structure of the activating IL-1 receptor signaling complex.,Thomas C, Bazan JF, Garcia KC Nat Struct Mol Biol. 2012 Mar 18;19(4):455-7. doi: 10.1038/nsmb.2260. PMID:22426547[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Slack JL, Schooley K, Bonnert TP, Mitcham JL, Qwarnstrom EE, Sims JE, Dower SK. Identification of two major sites in the type I interleukin-1 receptor cytoplasmic region responsible for coupling to pro-inflammatory signaling pathways. J Biol Chem. 2000 Feb 18;275(7):4670-8. PMID:10671496
- ↑ Thomas C, Bazan JF, Garcia KC. Structure of the activating IL-1 receptor signaling complex. Nat Struct Mol Biol. 2012 Mar 18;19(4):455-7. doi: 10.1038/nsmb.2260. PMID:22426547 doi:10.1038/nsmb.2260
