3O4O

Crystal structure of an Interleukin-1 receptor complex

Summary for 3O4O

• Entry DOI: 10.2210/pdb3o4o/pdb
• Descriptor: Interleukin-1 beta, Interleukin-1 receptor type 2, Interleukin-1 receptor accessory protein, ... (5 entities in total)
• Functional Keywords: cytokine-receptor complex, beta-trefoil, ig-like fold, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 97744.65

Authors

Wang, X.Q.,Wang, D.L.,Zhang, S.Y.,Li, L.,Liu, X.,Mei, K.R. (deposition date: 2010-07-27, release date: 2010-09-01, Last modification date: 2024-11-20)

Primary citation

Wang, D.L.,Zhang, S.Y.,Li, L.,Liu, X.,Mei, K.R.,Wang, X.Q.
Structural insights into the assembly and activation of IL-1beta with its receptors
Nat.Immunol., 11:905-911, 2010

PubMed Abstract: 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). How IL-1RAcP is recruited by IL-1β-IL-1RI to form the signaling-competent complex remains elusive. Here we present the crystal structure of IL-1β bound to IL-1 receptor type II (IL-1RII) and IL-1RAcP. IL-1β-IL-1RII generated a composite binding surface to recruit IL-1RAcP. Biochemical analysis demonstrated that IL-1β-IL-1RI and IL-1β-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.

PubMed: 20802483
DOI: 10.1038/ni.1925

Experimental method

X-RAY DIFFRACTION (3.3 Å)