This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ira
From Proteopedia
(New page: 200px<br /> <applet load="1ira" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ira, resolution 2.7Å" /> '''COMPLEX OF THE INTER...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ira.gif|left|200px]]<br /> | + | [[Image:1ira.gif|left|200px]]<br /><applet load="1ira" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ira" size=" | + | |
caption="1ira, resolution 2.7Å" /> | caption="1ira, resolution 2.7Å" /> | ||
'''COMPLEX OF THE INTERLEUKIN-1 RECEPTOR WITH THE INTERLEUKIN-1 RECEPTOR ANTAGONIST (IL1RA)'''<br /> | '''COMPLEX OF THE INTERLEUKIN-1 RECEPTOR WITH THE INTERLEUKIN-1 RECEPTOR ANTAGONIST (IL1RA)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Inflammation, regardless of whether it is provoked by infection or by | + | 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. |
==Disease== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1IRA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1IRA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRA OCA]. |
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Akeson, A.]] | [[Category: Akeson, A.]] | ||
| - | [[Category: Barrett, R | + | [[Category: Barrett, R W.]] |
[[Category: Bowlin, T.]] | [[Category: Bowlin, T.]] | ||
[[Category: Sarubbi, E.]] | [[Category: Sarubbi, E.]] | ||
| - | [[Category: Schreuder, H | + | [[Category: Schreuder, H A.]] |
[[Category: Soffientini, A.]] | [[Category: Soffientini, A.]] | ||
[[Category: Tardif, C.]] | [[Category: Tardif, C.]] | ||
| Line 32: | Line 31: | ||
[[Category: receptor antagonist]] | [[Category: receptor antagonist]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:50 2008'' |
Revision as of 11:14, 21 February 2008
|
COMPLEX OF THE INTERLEUKIN-1 RECEPTOR WITH THE INTERLEUKIN-1 RECEPTOR ANTAGONIST (IL1RA)
Contents |
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.
Disease
Known diseases associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147679], Mental retardation, X-linked, 21/34 OMIM:[300206]
About this Structure
1IRA is a Protein complex structure of sequences from Homo sapiens with as ligand. 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 Thu Feb 21 13:14:50 2008
