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Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1β

Author

Listed:
  • Guy P. A. Vigers

    (Amgen Inc.)

  • Lana J. Anderson

    (Amgen Inc.)

  • Patricia Caffes

    (Amgen Inc.)

  • Barbara J. Brandhuber

    (Amgen Inc.)

Abstract

Interleukin-1 (IL-1) is an important mediator of inflammatory disease. The IL-1 family currently consists of two agonists, IL-1α and IL-lβ, and one antagonist, IL-1ra. Each of these molecules binds to the type I IL-1 receptor (IL1R)1. The binding of IL-1α or IL-1β to IL1R is an early step in IL-1 signal transduction and blocking this interaction may therefore be a useful target for the development of new drugs. Here we report the three-dimensional structure of IL-1β bound to the extracellular domain of IL1R (s-IL1R) at 2.5Å resolution. IL-1β binds to s-IL1R with a 1:1 stoichiometry. The crystal structure shows that s-IL1R consists of three immunoglobulin-like domains which wrap around IL-1β in a manner distinct from the structures of previously described cytokine–receptor complexes. The two receptor-binding regions on IL-1β identified by site-directed mutagenesis2,3 both contact the receptor: one binds to the first two domains of the receptor, while the other binds exclusively to the third domain.

Suggested Citation

  • Guy P. A. Vigers & Lana J. Anderson & Patricia Caffes & Barbara J. Brandhuber, 1997. "Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1β," Nature, Nature, vol. 386(6621), pages 190-194, March.
    • Handle: RePEc:nat:nature:v:386:y:1997:i:6621:d:10.1038_386190a0
    DOI: 10.1038/386190a0
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    Cited by:

    1. Ulrich Hommel & Konstanze Hurth & Jean-Michel Rondeau & Anna Vulpetti & Daniela Ostermeier & Andreas Boettcher & Jacob Peter Brady & Michael Hediger & Sylvie Lehmann & Elke Koch & Anke Blechschmidt & , 2023. "Discovery of a selective and biologically active low-molecular weight antagonist of human interleukin-1β," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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