Structural highlights
Function
IL1B_HUMAN Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.[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
- ↑ Van Damme J, De Ley M, Opdenakker G, Billiau A, De Somer P, Van Beeumen J. Homogeneous interferon-inducing 22K factor is related to endogenous pyrogen and interleukin-1. Nature. 1985 Mar 21-27;314(6008):266-8. PMID:3920526
- ↑ 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
