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1ira
From Proteopedia
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[[Image:1ira.gif|left|200px]] | [[Image:1ira.gif|left|200px]] | ||
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'''COMPLEX OF THE INTERLEUKIN-1 RECEPTOR WITH THE INTERLEUKIN-1 RECEPTOR ANTAGONIST (IL1RA)''' | '''COMPLEX OF THE INTERLEUKIN-1 RECEPTOR WITH THE INTERLEUKIN-1 RECEPTOR ANTAGONIST (IL1RA)''' | ||
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[[Category: Tramp-Kalmeyer, S.]] | [[Category: Tramp-Kalmeyer, S.]] | ||
[[Category: Yanofsky, S.]] | [[Category: Yanofsky, S.]] | ||
| - | [[Category: | + | [[Category: Cytokine receptor]] |
| - | [[Category: | + | [[Category: Immunoglobulin fold]] |
| - | + | [[Category: Receptor antagonist]] | |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:19:06 2008'' |
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Revision as of 17:19, 2 May 2008
COMPLEX OF THE INTERLEUKIN-1 RECEPTOR WITH THE INTERLEUKIN-1 RECEPTOR ANTAGONIST (IL1RA)
Overview
Inflammation, regardless of whether it is provoked by infection or by tissue damage, starts with the activation of macrophages which initiate a cascade of inflammatory responses by producing the cytokines interleukin-1 (IL-1) and tumour necrosis factor-alpha (ref. 1). Three naturally occurring ligands for the IL-1 receptor (IL1R) exist: the agonists IL-1alpha and IL-1beta and the IL-1-receptor antagonist IL1RA (ref. 2). IL-1 is the only cytokine for which a naturally occurring antagonist is known. Here we describe the crystal structure at 2.7 A resolution of the soluble extracellular part of type-I IL1R complexed with IL1RA. The receptor consists of three immunoglobulin-like domains. Domains 1 and 2 are tightly linked, but domain three is completely separate and connected by a flexible linker. Residues of all three domains contact the antagonist and include the five critical IL1RA residues which were identified by site-directed mutagenesis. A region that is important for biological function in IL-1beta, the 'receptor trigger site' is not in direct contact with the receptor in the IL1RA complex. Modelling studies suggest that this IL-1beta trigger site might induce a movement of domain 3.
About this Structure
1IRA is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist., Schreuder H, Tardif C, Trump-Kallmeyer S, Soffientini A, Sarubbi E, Akeson A, Bowlin T, Yanofsky S, Barrett RW, Nature. 1997 Mar 13;386(6621):194-200. PMID:9062194 Page seeded by OCA on Fri May 2 20:19:06 2008
