1itb

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{{Seed}}
 
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[[Image:1itb.png|left|200px]]
 
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==TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA==
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The line below this paragraph, containing "STRUCTURE_1itb", creates the "Structure Box" on the page.
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<StructureSection load='1itb' size='340' side='right'caption='[[1itb]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1itb]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ITB FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1itb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1itb OCA], [https://pdbe.org/1itb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1itb RCSB], [https://www.ebi.ac.uk/pdbsum/1itb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1itb ProSAT]</span></td></tr>
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{{STRUCTURE_1itb| PDB=1itb | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IL1R1_HUMAN IL1R1_HUMAN] Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the corecptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex.<ref>PMID:10671496</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/it/1itb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1itb ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA===
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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<ref>PMID:9062193</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1itb" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_9062193}}, adds the Publication Abstract to the page
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*[[Interleukin 3D structures|Interleukin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9062193 is the PubMed ID number.
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*[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_9062193}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1ITB is a 2 chains 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].
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==Reference==
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<ref group="xtra">PMID:9062193</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Anderson, L J.]]
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[[Category: Large Structures]]
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[[Category: Brandhuber, B J.]]
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[[Category: Anderson LJ]]
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[[Category: Caffes, P.]]
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[[Category: Brandhuber BJ]]
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[[Category: Vigers, G P.A.]]
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[[Category: Caffes P]]
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[[Category: Glycoprotein]]
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[[Category: Vigers GPA]]
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[[Category: Immunoglobulin fold]]
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[[Category: Receptor]]
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[[Category: Signal]]
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[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 22:05:51 2009''
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Current revision

TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA

PDB ID 1itb

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