1g0y
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IL-1 RECEPTOR TYPE 1 COMPLEXED WITH ANTAGONIST PEPTIDE AF10847
OverviewOverview
Interleukin (IL-1)alpha and IL-1beta are important mediators of, inflammation. The binding of IL-1 to interleukin-1 receptor (IL-1R) type 1, is the initial step in IL-1 signal transduction and therefore is a, tempting target for anti-inflammatory therapeutics. To advance our, understanding of IL-1R1 binding interactions, we have determined the, structure of the extracellular domains of IL-1R1 bound to a 21-amino acid, IL-1 antagonist peptide at 3.0-A resolution. The antagonist peptide binds, to the domain 1/2 junction of the receptor, which is a conserved binding, site for IL-1beta and IL-1 receptor antagonist (IL-1ra). This co-crystal, structure also reveals that considerable flexibility is present in IL-1R1, because the carboxyl-terminal domain of the receptor is rotated almost 170, degrees relative to the first two domains of the receptor compared with, the previously solved IL-1R1.ligand structures. The structure shows an, unexpected binding mode for the peptide and may contribute to the design, of smaller IL-1R antagonists.
DiseaseDisease
Known diseases associated with this structure: Mental retardation, X-linked, 21/34 OMIM:[300206]
About this StructureAbout this Structure
1G0Y is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
X-ray crystal structure of a small antagonist peptide bound to interleukin-1 receptor type 1., Vigers GP, Dripps DJ, Edwards CK 3rd, Brandhuber BJ, J Biol Chem. 2000 Nov 24;275(47):36927-33. PMID:10903327
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