1ITB

TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA

Summary for 1ITB

• Entry DOI: 10.2210/pdb1itb/pdb
• Descriptor: INTERLEUKIN-1 BETA, TYPE 1 INTERLEUKIN-1 RECEPTOR (3 entities in total)
• Functional Keywords: immunoglobulin fold, transmembrane, glycoprotein, receptor, complex (immunoglobulin-receptor), complex (immunoglobulin-receptor) complex, complex (immunoglobulin/receptor)
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P01584; Membrane; Single-pass type I membrane protein: P14778
• Total number of polymer chains: 2
• Total formula weight: 53618.98

Authors

Vigers, G.P.A.,Anderson, L.J.,Caffes, P.,Brandhuber, B.J. (deposition date: 1997-01-15, release date: 1998-02-04, Last modification date: 2024-10-23)

Primary citation

Vigers, G.P.,Anderson, L.J.,Caffes, P.,Brandhuber, B.J.
Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta.
Nature, 386:190-194, 1997

PubMed Abstract: 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.

PubMed: 9062193
DOI: 10.1038/386190a0

Experimental method

X-RAY DIFFRACTION (2.5 Å)