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2ers
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="2ers" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ers" /> '''Solution structure of the Interleukin-15 re...) |
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| - | [[Image:2ers.gif|left|200px]]<br /> | ||
| - | <applet load="2ers" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2ers" /> | ||
| - | '''Solution structure of the Interleukin-15 receptor sushi domain'''<br /> | ||
| - | == | + | ==Solution structure of the Interleukin-15 receptor sushi domain== |
| - | + | <StructureSection load='2ers' size='340' side='right'caption='[[2ers]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | [[ | + | <table><tr><td colspan='2'>[[2ers]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ERS FirstGlance]. <br> |
| - | [[ | + | </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=2ers FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ers OCA], [https://pdbe.org/2ers PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ers RCSB], [https://www.ebi.ac.uk/pdbsum/2ers PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ers ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | [[ | + | == Function == |
| - | [[ | + | [[https://www.uniprot.org/uniprot/I15RA_HUMAN I15RA_HUMAN]] High-affinity receptor for interleukin-15. Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. Expression of different isoforms may alter or interfere with signal transduction. Isoform 5, isoform 6, isoform 7 and isoform 8 do not bind IL15. Signal transduction involves STAT3, STAT5, STAT6, JAK2 (By similarity) and SYK.<ref>PMID:8530383</ref> <ref>PMID:11714793</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/er/2ers_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2ers ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Interleukin (IL)-15 is a member of the small four alpha-helix bundle family of cytokines. IL-15 was discovered by its ability to mimic IL-2-mediated T-cell proliferation. Both cytokines share the beta and gamma receptor chains of the IL-2 receptor for signal transduction. However, in addition, they target specific alpha chain receptors IL-15Ralpha and IL-2Ralpha, respectively. The exceptionally high affinity binding of IL-15 to IL-15Ralpha is mediated by its sushi domain. Here we present the solution structure of the IL-15Ralpha sushi domain solved by NMR spectroscopy and a model of its complex with IL-15. The model shows that, rather than the familiar hydrophobic forces dominating the interaction interface between cytokines and their cognate receptors, the interaction between the IL-15 and IL-15Ralpha complex involves a large network of ionic interactions. This type of interaction explains the exceptionally high affinity of the IL-15.IL-15Ralpha complex, which is essential for the biological effects of this important cytokine and which is not observed in other cytokine/cytokine receptor complexes. | ||
| - | + | The structure of the interleukin-15 alpha receptor and its implications for ligand binding.,Lorenzen I, Dingley AJ, Jacques Y, Grotzinger J J Biol Chem. 2006 Mar 10;281(10):6642-7. Epub 2005 Dec 23. PMID:16377614<ref>PMID:16377614</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2ers" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dingley, A J]] | ||
| + | [[Category: Grotzinger, J]] | ||
| + | [[Category: Lorenzen, I]] | ||
| + | [[Category: Signaling protein]] | ||
| + | [[Category: Sushi domain]] | ||
Current revision
Solution structure of the Interleukin-15 receptor sushi domain
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