2l5x
From Proteopedia
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== Function == | == Function == | ||
[[http://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. [[http://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> | [[http://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. [[http://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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:21270123</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2l5x" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Revision as of 12:15, 13 January 2016
Solution structure of IL1A-S100A13 complex
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