PMID: 20802483

 

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Title : Structural insights into the assembly and activation of IL-1β with its receptors

Abstract :
  1. Interleukin 1β ( IL-1β) 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 )
  2. How IL-1RAcP is recruited by IL-1β- IL-1RI to form the signaling-competent complex remains elusive
  3. Here we present the crystal structure of IL-1β bound to IL-1 receptor type II ( IL-1RII ) and IL-1RAcP
  4. IL-1β- IL-1RII generated a composite binding surface to recruit IL-1RAcP
  5. Biochemical analysis demonstrated that IL-1β- IL-1RI and IL-1β- IL-1RII interacted similarly with IL-1RAcP
  6. It also showed the importance of two loops of IL-1 receptor antagonist ( IL-1Ra ) in determining its antagonism
  7. 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