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|1itb, resolution 2.50Å ()|
TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA
Interleukin-1 (IL-1) is an important mediator of inflammatory disease. The IL-1 family currently consists of two agonists, IL-1alpha and IL-1beta, and one antagonist, IL-1ra. Each of these molecules binds to the type I IL-1 receptor (IL1R). The binding of IL-1alpha or IL-1beta 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-1beta bound to the extracellular domain of IL1R (s-IL1R) at 2.5 A resolution. IL-1beta 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-1beta in a manner distinct from the structures of previously described cytokine-receptor complexes. The two receptor-binding regions on IL-1beta identified by site-directed mutagenesis both contact the receptor: one binds to the first two domains of the receptor, while the other binds exclusively to the third domain.
Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta., Vigers GP, Anderson LJ, Caffes P, Brandhuber BJ, Nature. 1997 Mar 13;386(6621):190-4. PMID:9062193
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Vigers GP, Anderson LJ, Caffes P, Brandhuber BJ. Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta. Nature. 1997 Mar 13;386(6621):190-4. PMID:9062193 doi:10.1038/386190a0
- Kato Z, Jee J, Shikano H, Mishima M, Ohki I, Ohnishi H, Li A, Hashimoto K, Matsukuma E, Omoya K, Yamamoto Y, Yoneda T, Hara T, Kondo N, Shirakawa M. The structure and binding mode of interleukin-18. Nat Struct Biol. 2003 Nov;10(11):966-71. Epub 2003 Oct 5. PMID:14528293 doi:10.1038/nsb993