3O4O: Crystal Structure Of An Interleukin-1 Receptor Complex

Interleukin 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.
PDB ID: 3O4ODownload
MMDB ID: 84580
PDB Deposition Date: 2010/7/27
Updated in MMDB: 2010/10
Experimental Method:
x-ray diffraction
Resolution: 3.3  Å
Source Organism:
Similar Structures:
Biological Unit for 3O4O: trimeric; determined by software (PISA)
Molecular Components in 3O4O
Label Count Molecule
Proteins (3 molecules)
Interleukin-1 Beta(Gene symbol: IL1B)
Molecule annotation
Interleukin-1 Receptor Type 2(Gene symbol: IL1R2)
Molecule annotation
Interleukin-1 Receptor Accessory Protein(Gene symbol: IL1RAP)
Molecule annotation
Chemicals (8 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB