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| [[Image:1g0y.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1g0y| PDB=1g0y | SCENE= }} | | {{STRUCTURE_1g0y| PDB=1g0y | SCENE= }} |
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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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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10903327}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10903327 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10903327}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Vigers, G P.A.]] | | [[Category: Vigers, G P.A.]] |
| [[Category: Immunoglobulin]] | | [[Category: Immunoglobulin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:59:42 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:14:24 2008'' |