1y6n
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:1y6n.png|left|200px]] | ||
| - | + | ==Crystal structure of Epstein-Barr virus IL-10 mutant (A87I) complexed with the soluble IL-10R1 chain== | |
| - | + | <StructureSection load='1y6n' size='340' side='right'caption='[[1y6n]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1y6n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_4 Human gammaherpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y6N 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]] 2.7Å</td></tr> | |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1y6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y6n OCA], [https://pdbe.org/1y6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y6n RCSB], [https://www.ebi.ac.uk/pdbsum/1y6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y6n ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/IL10H_EBVB9 IL10H_EBVB9] Plays a role in masking infected cells for immune recognition by cytotoxic T-lymphocytes. Down-regulates the expression of the host TAP1 gene (transporter associated with antigen processing), thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules. Inhibits IFN-gamma synthesis.<ref>PMID:2161559</ref> <ref>PMID:9310490</ref> | ||
| + | == 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/y6/1y6n_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=1y6n ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human IL-10 (hIL-10) is a cytokine that modulates diverse immune responses. The Epstein-Barr virus (EBV) genome contains an IL-10 homolog (vIL-10) that shares high sequence and structural similarity with hIL-10. Although vIL-10 suppresses inflammatory responses like hIL-10, it cannot activate many other immunostimulatory functions performed by the cellular cytokine. These functional differences have been correlated with the approximately 1000-fold lower affinity of vIL-10, compared to hIL-10, for the IL-10R1 receptor chain. To define the structural basis for these observations, crystal structures of vIL-10 and a vIL-10 point mutant were determined bound to the soluble IL-10R1 receptor fragment (sIL-10R1) at 2.8 and 2.7 A resolution, respectively. The structures reveal that subtle changes in the conformation and dynamics of the vIL-10 AB and CD loops and an orientation change of vIL-10 on sIL-10R1 are the main factors responsible for vIL-10's reduced affinity for sIL-10R1 and its distinct biological profile. | ||
| - | + | Same structure, different function crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain.,Yoon SI, Jones BC, Logsdon NJ, Walter MR Structure. 2005 Apr;13(4):551-64. PMID:15837194<ref>PMID:15837194</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1y6n" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Interleukin 3D structures|Interleukin 3D structures]] | |
| - | + | *[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
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| - | == | + | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Human | + | [[Category: Human gammaherpesvirus 4]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Jones | + | [[Category: Jones BC]] |
| - | [[Category: Logsdon | + | [[Category: Logsdon NJ]] |
| - | [[Category: Walter | + | [[Category: Walter MR]] |
| - | [[Category: Yoon | + | [[Category: Yoon SI]] |
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Current revision
Crystal structure of Epstein-Barr virus IL-10 mutant (A87I) complexed with the soluble IL-10R1 chain
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