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New page: left|200px<br /> <applet load="1j7v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j7v, resolution 2.9Å" /> '''HUMAN IL-10 / IL-10R...
 
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[[Image:1j7v.gif|left|200px]]<br />
<applet load="1j7v" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1j7v, resolution 2.9&Aring;" />
'''HUMAN IL-10 / IL-10R1 COMPLEX'''<br />


==Overview==
==HUMAN IL-10 / IL-10R1 COMPLEX==
Interleukin 10 (IL-10) is a dimeric cytokine that plays a central role in, suppressing inflammatory responses. These activities are dependent on the, interaction of IL-10 with its high-affinity receptor (IL-10R1). This, intermediate complex must subsequently recruit the low-affinity IL-10R2, chain before cell signaling can occur. Here we report the 2.9 A crystal, structure of IL-10 bound to a soluble form of IL-10R1 (sIL-10R1). The, complex consists of two IL-10s and four sIL-10R1 molecules. Several, residues in the IL-10/sIL-10R1 interface are conserved in all IL-10, homologs and their receptors. The data suggests that formation of the, active IL-10 signaling complex occurs by a novel molecular recognition, paradigm where IL-10R1 and IL-10R2 both recognize the same binding site on, IL-10.
<StructureSection load='1j7v' size='340' side='right'caption='[[1j7v]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1j7v]] 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=1J7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J7V FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j7v OCA], [https://pdbe.org/1j7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j7v RCSB], [https://www.ebi.ac.uk/pdbsum/1j7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j7v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IL10_HUMAN IL10_HUMAN] Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j7/1j7v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1j7v ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Interleukin 10 (IL-10) is a dimeric cytokine that plays a central role in suppressing inflammatory responses. These activities are dependent on the interaction of IL-10 with its high-affinity receptor (IL-10R1). This intermediate complex must subsequently recruit the low-affinity IL-10R2 chain before cell signaling can occur. Here we report the 2.9 A crystal structure of IL-10 bound to a soluble form of IL-10R1 (sIL-10R1). The complex consists of two IL-10s and four sIL-10R1 molecules. Several residues in the IL-10/sIL-10R1 interface are conserved in all IL-10 homologs and their receptors. The data suggests that formation of the active IL-10 signaling complex occurs by a novel molecular recognition paradigm where IL-10R1 and IL-10R2 both recognize the same binding site on IL-10.


==Disease==
Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site.,Josephson K, Logsdon NJ, Walter MR Immunity. 2001 Jul;15(1):35-46. PMID:11485736<ref>PMID:11485736</ref>
Known diseases associated with this structure: Graft-versus-host disease, protection against OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=124092 124092]], HIV-1, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=124092 124092]], Rheumatoid arthritis, progression of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=124092 124092]]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1J7V 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J7V OCA].
</div>
<div class="pdbe-citations 1j7v" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site., Josephson K, Logsdon NJ, Walter MR, Immunity. 2001 Jul;15(1):35-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11485736 11485736]
*[[Interleukin 3D structures|Interleukin 3D structures]]
*[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Josephson, K.]]
[[Category: Josephson K]]
[[Category: Logsdon, N.]]
[[Category: Logsdon N]]
[[Category: Walter, M.R.]]
[[Category: Walter MR]]
[[Category: 4 helix bundle]]
[[Category: class 2 receptor]]
[[Category: cytokine receptor complex]]
[[Category: interleukin-10]]
 
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