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| | ==Solution structure of IL1A-S100A13 complex== | | ==Solution structure of IL1A-S100A13 complex== |
| - | <StructureSection load='2l5x' size='340' side='right'caption='[[2l5x]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2l5x' size='340' side='right'caption='[[2l5x]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l5x]] is a 4 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=2L5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L5X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l5x]] is a 4 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=2L5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L5X FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IL1A, IL1F1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), S100A13 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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=2l5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l5x OCA], [https://pdbe.org/2l5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l5x RCSB], [https://www.ebi.ac.uk/pdbsum/2l5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l5x ProSAT]</span></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=2l5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l5x OCA], [https://pdbe.org/2l5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l5x RCSB], [https://www.ebi.ac.uk/pdbsum/2l5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l5x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/IL1A_HUMAN IL1A_HUMAN]] Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. [[https://www.uniprot.org/uniprot/S10AD_HUMAN S10AD_HUMAN]] Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity).<ref>PMID:12746488</ref> <ref>PMID:20863990</ref>
| + | [https://www.uniprot.org/uniprot/IL1A_HUMAN IL1A_HUMAN] Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mohan, S K]] | + | [[Category: Mohan SK]] |
| - | [[Category: Yu, C]] | + | [[Category: Yu C]] |
| - | [[Category: Cytokine-transport protein complex]]
| + | |
| - | [[Category: Interleukin-1alpha]]
| + | |
| - | [[Category: Key component in non-classical pathway of il-1a]]
| + | |
| - | [[Category: Protein-protein complex]]
| + | |
| - | [[Category: S100a13]]
| + | |
| Structural highlights
Function
IL1A_HUMAN Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
Publication Abstract from PubMed
Interleukin 1alpha (IL1alpha) plays an important role in several key biological functions, such as angiogenesis, cell proliferation, and tumor growth in several types of cancer. IL1alpha is a potent cytokine that induces a wide spectrum of immunological and inflammatory activities. The biological effects of IL1alpha are mediated through the activation of transmembrane receptors (IL1Rs) and therefore require the release of the protein into the extracellular space. IL1alpha is exported through a non-classical release pathway involving the formation of a specific multiprotein complex, which includes IL1alpha and S100A13. Because IL1alpha plays an important role in cell proliferation and angiogenesis, inhibiting the formation of the IL1alpha-S100A13 complex would be an effective strategy to inhibit a wide range of cancers. To understand the molecular events in the IL1alpha release pathway, we studied the structure of the IL1alpha-S100A13 tetrameric complex, which is the key complex formed during the non-classical pathway of IL1alpha release.
The IL1alpha-S100A13 heterotetrameric complex structure: a component in the non-classical pathway for interleukin 1alpha secretion.,Mohan SK, Yu C J Biol Chem. 2011 Apr 22;286(16):14608-17. Epub 2011 Jan 26. PMID:21270123[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mohan SK, Yu C. The IL1alpha-S100A13 heterotetrameric complex structure: a component in the non-classical pathway for interleukin 1alpha secretion. J Biol Chem. 2011 Apr 22;286(16):14608-17. Epub 2011 Jan 26. PMID:21270123 doi:http://dx.doi.org/10.1074/jbc.M110.201954
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