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1j0s

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Solution structure of the human interleukin-18

Structural highlights

1j0s 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
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IL18_HUMAN Augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells.

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-18 (IL-18), a cytokine formerly known as interferon-gamma- (IFN-gamma-) inducing factor, has pleiotropic immunoregulatory functions, including augmentation of IFN-gamma production, Fas-mediated cytotoxicity and developmental regulation of T-lymphocyte helper type I. We determined the solution structure of IL-18 as a first step toward understanding its receptor activation mechanism. It folds into a beta-trefoil structure that resembles that of IL-1. Extensive mutagenesis revealed the presence of three sites that are important for receptor activation: two serve as binding sites for IL-18 receptor alpha (IL-18Ralpha), located at positions similar to those of IL-1 for IL-1 receptor type I (IL-1RI), whereas the third site may be involved in IL-18 receptor beta (IL-18Rbeta) binding. The structure and mutagenesis data provide a basis for understanding the IL-18-induced heterodimerization of receptor subunits, which is necessary for receptor activation.

The structure and binding mode of interleukin-18.,Kato Z, Jee J, Shikano H, Mishima M, Ohki I, Ohnishi H, Li A, Hashimoto K, Matsukuma E, Omoya K, Yamamoto Y, Yoneda T, Hara T, Kondo N, Shirakawa M Nat Struct Biol. 2003 Nov;10(11):966-71. Epub 2003 Oct 5. PMID:14528293^[1]

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

References

↑ Kato Z, Jee J, Shikano H, Mishima M, Ohki I, Ohnishi H, Li A, Hashimoto K, Matsukuma E, Omoya K, Yamamoto Y, Yoneda T, Hara T, Kondo N, Shirakawa M. The structure and binding mode of interleukin-18. Nat Struct Biol. 2003 Nov;10(11):966-71. Epub 2003 Oct 5. PMID:14528293 doi:10.1038/nsb993

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/1j0s"

@@ Line 1: / Line 1: @@
 ==Solution structure of the human interleukin-18==
-<StructureSection load='1j0s' size='340' side='right'caption='[[1j0s]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1j0s' size='340' side='right'caption='[[1j0s]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1j0s]] 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=1J0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J0S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1j0s]] 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=1J0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J0S 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=1j0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j0s OCA], [https://pdbe.org/1j0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j0s RCSB], [https://www.ebi.ac.uk/pdbsum/1j0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j0s ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1j0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j0s OCA], [https://pdbe.org/1j0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j0s RCSB], [https://www.ebi.ac.uk/pdbsum/1j0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j0s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/IL18_HUMAN IL18_HUMAN]] Augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells.
+[https://www.uniprot.org/uniprot/IL18_HUMAN IL18_HUMAN] Augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Hara, T]]
+[[Category: Hara T]]
-[[Category: Jee, J]]
+[[Category: Jee J]]
-[[Category: Kato, Z]]
+[[Category: Kato Z]]
-[[Category: Kondo, N]]
+[[Category: Kondo N]]
-[[Category: Mishima, M]]
+[[Category: Mishima M]]
-[[Category: Ohki, I]]
+[[Category: Ohki I]]
-[[Category: Shikano, H]]
+[[Category: Shikano H]]
-[[Category: Shirakawa, M]]
+[[Category: Shirakawa M]]
-[[Category: Torigoe, K]]
+[[Category: Torigoe K]]
-[[Category: Yoneda, T]]
+[[Category: Yoneda T]]
-[[Category: Beta trefoil]]
-[[Category: Cytokine]]

1j0s

From Proteopedia

Current revision

Solution structure of the human interleukin-18

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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