2ers

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the Interleukin-15 receptor sushi domain

Structural highlights

2ers is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 1 model
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Anderson DM, Kumaki S, Ahdieh M, Bertles J, Tometsko M, Loomis A, Giri J, Copeland NG, Gilbert DJ, Jenkins NA, et al.. Functional characterization of the human interleukin-15 receptor alpha chain and close linkage of IL15RA and IL2RA genes. J Biol Chem. 1995 Dec 15;270(50):29862-9. PMID:8530383
↑ Bulanova E, Budagian V, Pohl T, Krause H, Durkop H, Paus R, Bulfone-Paus S. The IL-15R alpha chain signals through association with Syk in human B cells. J Immunol. 2001 Dec 1;167(11):6292-302. PMID:11714793
↑ Lorenzen I, Dingley AJ, Jacques Y, Grotzinger J. The structure of the interleukin-15 alpha receptor and its implications for ligand binding. J Biol Chem. 2006 Mar 10;281(10):6642-7. Epub 2005 Dec 23. PMID:16377614 doi:10.1074/jbc.M513118200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ers"

Categories: Homo sapiens | Large Structures | Dingley AJ | Grotzinger J | Lorenzen I

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:2ers.png|left|200px]]
-<!--
+==Solution structure of the Interleukin-15 receptor sushi domain==
-The line below this paragraph, containing "STRUCTURE_2ers", creates the "Structure Box" on the page.
+<StructureSection load='2ers' size='340' side='right'caption='[[2ers]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2ers]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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>
-{{STRUCTURE_2ers|  PDB=2ers  |  SCENE=  }}
+</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/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=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.
-===Solution structure of the Interleukin-15 receptor sushi domain===
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2ers" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16377614}}, adds the Publication Abstract to the page
+*[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16377614 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16377614}}
+__TOC__
+</StructureSection>
-==About this Structure==
-ERS is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERS OCA].
-==Reference==
-<ref group="xtra">PMID:16377614</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Dingley, A J.]]
+[[Category: Large Structures]]
-[[Category: Grotzinger, J.]]
+[[Category: Dingley AJ]]
-[[Category: Lorenzen, I.]]
+[[Category: Grotzinger J]]
-[[Category: Signaling protein]]
+[[Category: Lorenzen I]]
-[[Category: Sushi domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 21:23:37 2009''

2ers

From Proteopedia

Current revision

Solution structure of the Interleukin-15 receptor sushi domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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