1itb: Difference between revisions
New page: left|200px<br /> <applet load="1itb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1itb, resolution 2.5Å" /> '''TYPE-1 INTERLEUKIN-1... |
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[[Image:1itb.gif|left|200px]]<br /> | [[Image:1itb.gif|left|200px]]<br /><applet load="1itb" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1itb, resolution 2.5Å" /> | caption="1itb, resolution 2.5Å" /> | ||
'''TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA'''<br /> | '''TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA'''<br /> | ||
==Overview== | ==Overview== | ||
Interleukin-1 (IL-1) is an important mediator of inflammatory disease. The | Interleukin-1 (IL-1) is an important mediator of inflammatory disease. The IL-1 family currently consists of two agonists, IL-1alpha and IL-1beta, and one antagonist, IL-1ra. Each of these molecules binds to the type I IL-1 receptor (IL1R). The binding of IL-1alpha or IL-1beta to IL1R is an early step in IL-1 signal transduction and blocking this interaction may therefore be a useful target for the development of new drugs. Here we report the three-dimensional structure of IL-1beta bound to the extracellular domain of IL1R (s-IL1R) at 2.5 A resolution. IL-1beta binds to s-IL1R with a 1:1 stoichiometry. The crystal structure shows that s-IL1R consists of three immunoglobulin-like domains which wrap around IL-1beta in a manner distinct from the structures of previously described cytokine-receptor complexes. The two receptor-binding regions on IL-1beta identified by site-directed mutagenesis both contact the receptor: one binds to the first two domains of the receptor, while the other binds exclusively to the third domain. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1ITB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1ITB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ITB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Anderson, L | [[Category: Anderson, L J.]] | ||
[[Category: Brandhuber, B | [[Category: Brandhuber, B J.]] | ||
[[Category: Caffes, P.]] | [[Category: Caffes, P.]] | ||
[[Category: Vigers, G | [[Category: Vigers, G P.A.]] | ||
[[Category: complex (immunoglobulin/receptor)]] | [[Category: complex (immunoglobulin/receptor)]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:25 2008'' | ||
Revision as of 14:15, 21 February 2008
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TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA
OverviewOverview
Interleukin-1 (IL-1) is an important mediator of inflammatory disease. The IL-1 family currently consists of two agonists, IL-1alpha and IL-1beta, and one antagonist, IL-1ra. Each of these molecules binds to the type I IL-1 receptor (IL1R). The binding of IL-1alpha or IL-1beta to IL1R is an early step in IL-1 signal transduction and blocking this interaction may therefore be a useful target for the development of new drugs. Here we report the three-dimensional structure of IL-1beta bound to the extracellular domain of IL1R (s-IL1R) at 2.5 A resolution. IL-1beta binds to s-IL1R with a 1:1 stoichiometry. The crystal structure shows that s-IL1R consists of three immunoglobulin-like domains which wrap around IL-1beta in a manner distinct from the structures of previously described cytokine-receptor complexes. The two receptor-binding regions on IL-1beta identified by site-directed mutagenesis both contact the receptor: one binds to the first two domains of the receptor, while the other binds exclusively to the third domain.
DiseaseDisease
Known diseases associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147720], Mental retardation, X-linked, 21/34 OMIM:[300206]
About this StructureAbout this Structure
1ITB is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta., Vigers GP, Anderson LJ, Caffes P, Brandhuber BJ, Nature. 1997 Mar 13;386(6621):190-4. PMID:9062193
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