SUMO conjugating enzyme Ubc9
From Proteopedia
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- | + | <StructureSection load='2gjd' size='350' side='right' scene='SUMO_conjugating_enzyme_Ubc9/Cv/1' caption='SUMO conjugating enzyme Ubc9 tetramer [[2gjd]]> | |
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== Function == | == Function == | ||
[[SUMO conjugating enzyme Ubc9]] accepts the ubiquitin-like SUMOs and catalyzes their attachment to other proteins with the help of E3 ligase<ref>PMID:23644018</ref>. | [[SUMO conjugating enzyme Ubc9]] accepts the ubiquitin-like SUMOs and catalyzes their attachment to other proteins with the help of E3 ligase<ref>PMID:23644018</ref>. | ||
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== Relevance == | == Relevance == | ||
Ubc9 inhibitors may be therapeutic agents against fibrotic diseases like rheumatoid arthritis<ref>PMID:22904261</ref><ref>PMID:24531852</ref>. | Ubc9 inhibitors may be therapeutic agents against fibrotic diseases like rheumatoid arthritis<ref>PMID:22904261</ref><ref>PMID:24531852</ref>. | ||
- | + | </StructureSection> | |
== 3D Structures of SUMO conjugating enzyme Ubc9 == | == 3D Structures of SUMO conjugating enzyme Ubc9 == | ||
Revision as of 09:55, 14 June 2017
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3D Structures of SUMO conjugating enzyme Ubc9
Updated on 14-June-2017
References
- ↑ Klug H, Xaver M, Chaugule VK, Koidl S, Mittler G, Klein F, Pichler A. Ubc9 sumoylation controls SUMO chain formation and meiotic synapsis in Saccharomyces cerevisiae. Mol Cell. 2013 Jun 6;50(5):625-36. doi: 10.1016/j.molcel.2013.03.027. Epub 2013, May 2. PMID:23644018 doi:http://dx.doi.org/10.1016/j.molcel.2013.03.027
- ↑ Khodzhigorova A, Distler A, Lang V, Dees C, Schneider H, Beyer C, Gelse K, Distler O, Schett G, Distler JH. Inhibition of sumoylation prevents experimental fibrosis. Ann Rheum Dis. 2012 Nov;71(11):1904-8. doi: 10.1136/annrheumdis-2012-201746. Epub, 2012 Aug 17. PMID:22904261 doi:http://dx.doi.org/10.1136/annrheumdis-2012-201746
- ↑ Li F, Li X, Kou L, Li Y, Meng F, Ma F. SUMO-conjugating enzyme UBC9 promotes proliferation and migration of fibroblast-like synoviocytes in rheumatoid arthritis. Inflammation. 2014 Aug;37(4):1134-41. doi: 10.1007/s10753-014-9837-x. PMID:24531852 doi:http://dx.doi.org/10.1007/s10753-014-9837-x