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4kc3

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{{STRUCTURE_4kc3| PDB=4kc3 | SCENE= }}
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==Cytokine/receptor binary complex==
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===Cytokine/receptor binary complex===
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<StructureSection load='4kc3' size='340' side='right' caption='[[4kc3]], [[Resolution|resolution]] 3.27&Aring;' scene=''>
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{{ABSTRACT_PUBMED_23980170}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4kc3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rhizobium_loessense Rhizobium loessense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KC3 FirstGlance]. <br>
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==Function==
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IL33, C9orf26, IL1F11, NFHEV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), IL1RL1, DER4, ST2, T1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158890 Rhizobium loessense])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kc3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kc3 RCSB], [http://www.ebi.ac.uk/pdbsum/4kc3 PDBsum]</span></td></tr>
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</table>
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== Function ==
[[http://www.uniprot.org/uniprot/IL33_HUMAN IL33_HUMAN]] Cytokine that binds to and signals through IL1RL1/ST2 and its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Induces T-helper type 2-associated cytokines. Acts as a chemoattractant tor Th2 cells, and may function as an "alarmin", that amplifies immune responses during tissue injury.<ref>PMID:16286016</ref> <ref>PMID:17853410</ref> <ref>PMID:17185418</ref> <ref>PMID:18787100</ref> <ref>PMID:18836528</ref> <ref>PMID:21734074</ref> <ref>PMID:22215666</ref> In quiescent endothelia the uncleaved form is constitutively and abundantly expressed, and acts as a chromatin-associated nuclear factor with transcriptional repressor properties, it may sequester nuclear NF-kappaB/RELA, lowering expression of its targets. This form is rapidely lost upon angiogenic or proinflammatory activation.<ref>PMID:16286016</ref> <ref>PMID:17853410</ref> <ref>PMID:17185418</ref> <ref>PMID:18787100</ref> <ref>PMID:18836528</ref> <ref>PMID:21734074</ref> <ref>PMID:22215666</ref> [[http://www.uniprot.org/uniprot/ILRL1_HUMAN ILRL1_HUMAN]] Receptor for interleukin-33 (IL-33), its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in helper T-cell function.<ref>PMID:16286016</ref>
[[http://www.uniprot.org/uniprot/IL33_HUMAN IL33_HUMAN]] Cytokine that binds to and signals through IL1RL1/ST2 and its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Induces T-helper type 2-associated cytokines. Acts as a chemoattractant tor Th2 cells, and may function as an "alarmin", that amplifies immune responses during tissue injury.<ref>PMID:16286016</ref> <ref>PMID:17853410</ref> <ref>PMID:17185418</ref> <ref>PMID:18787100</ref> <ref>PMID:18836528</ref> <ref>PMID:21734074</ref> <ref>PMID:22215666</ref> In quiescent endothelia the uncleaved form is constitutively and abundantly expressed, and acts as a chromatin-associated nuclear factor with transcriptional repressor properties, it may sequester nuclear NF-kappaB/RELA, lowering expression of its targets. This form is rapidely lost upon angiogenic or proinflammatory activation.<ref>PMID:16286016</ref> <ref>PMID:17853410</ref> <ref>PMID:17185418</ref> <ref>PMID:18787100</ref> <ref>PMID:18836528</ref> <ref>PMID:21734074</ref> <ref>PMID:22215666</ref> [[http://www.uniprot.org/uniprot/ILRL1_HUMAN ILRL1_HUMAN]] Receptor for interleukin-33 (IL-33), its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in helper T-cell function.<ref>PMID:16286016</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease. It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family. To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 A. Coupled with structure-based mutagenesis and binding assay, the structural results define the molecular mechanism by which ST2 specifically recognizes IL-33. Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors. Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution. The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly. The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis resembles IL-1beta-IL-1RII-IL-1RAcP and IL-1beta-IL-1RI-IL-1RAcP crystal structures. The collective results confer IL-33 structure-function relationships, supporting and extending a general model for ligand-receptor assembly and activation in the IL-1 family.
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==About this Structure==
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Structural insights into the interaction of IL-33 with its receptors.,Liu X, Hammel M, He Y, Tainer JA, Jeng US, Zhang L, Wang S, Wang X Proc Natl Acad Sci U S A. 2013 Sep 10;110(37):14918-23. doi:, 10.1073/pnas.1308651110. Epub 2013 Aug 26. PMID:23980170<ref>PMID:23980170</ref>
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[[4kc3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rhizobium_loessense Rhizobium loessense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KC3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:023980170</ref><references group="xtra"/><references/>
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</div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Rhizobium loessense]]
[[Category: Rhizobium loessense]]
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[[Category: Liu, X.]]
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[[Category: Liu, X]]
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[[Category: Wang, X Q.]]
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[[Category: Wang, X Q]]
[[Category: Beta-trefoil]]
[[Category: Beta-trefoil]]
[[Category: Ig-like domain]]
[[Category: Ig-like domain]]
[[Category: Immune system]]
[[Category: Immune system]]

Revision as of 22:17, 24 December 2014

Cytokine/receptor binary complex

4kc3, resolution 3.27Å

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