1itb
From Proteopedia
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TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA
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Overview
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.
Disease
Known diseases associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147720], Mental retardation, X-linked, 21/34 OMIM:[300206]
About this Structure
1ITB is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:15:25 2008
