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Crystal structure of an Interleukin-1 receptor complex
Structural highlights
FunctionIL1B_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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedInterleukin 1beta (IL-1beta) is a key orchestrator of inflammation and host defense that exerts its effects through IL-1 receptor type I (IL-1RI) and IL-1 receptor accessory protein (IL-1RAcP). How IL-1RAcP is recruited by IL-1beta-IL-1RI to form the signaling-competent complex remains elusive. Here we present the crystal structure of IL-1beta bound to IL-1 receptor type II (IL-1RII) and IL-1RAcP. IL-1beta-IL-1RII generated a composite binding surface to recruit IL-1RAcP. Biochemical analysis demonstrated that IL-1beta-IL-1RI and IL-1beta-IL-1RII interacted similarly with IL-1RAcP. It also showed the importance of two loops of IL-1 receptor antagonist (IL-1Ra) in determining its antagonism. Our results provide a structural basis for assembly and activation of the IL-1 receptor and offer a general cytokine-receptor architecture that governs the IL-1 family of cytokines. Structural insights into the assembly and activation of IL-1beta with its receptors.,Wang D, Zhang S, Li L, Liu X, Mei K, Wang X Nat Immunol. 2010 Aug 29. PMID:20802483[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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