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'''IL-1 RECEPTOR TYPE 1 COMPLEXED WITH ANTAGONIST PEPTIDE AF10847''' | '''IL-1 RECEPTOR TYPE 1 COMPLEXED WITH ANTAGONIST PEPTIDE AF10847''' | ||
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[[Category: Edwards, C K.]] | [[Category: Edwards, C K.]] | ||
[[Category: Vigers, G P.A.]] | [[Category: Vigers, G P.A.]] | ||
[[Category: | [[Category: Immunoglobulin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:59:42 2008'' | |||
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Revision as of 16:59, 2 May 2008
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.
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 Page seeded by OCA on Fri May 2 16:59:42 2008