2mp2: Difference between revisions
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mp2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mp2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mp2 PDBsum]</span></td></tr> | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mp2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mp2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mp2 PDBsum]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which targets substrates for proteasomal degradation. Here we use a segmental labelling approach combined with solution nuclear magnetic resonance (NMR) spectroscopy and biochemical characterization to reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer. | |||
Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4.,Xu Y, Plechanovova A, Simpson P, Marchant J, Leidecker O, Kraatz S, Hay RT, Matthews SJ Nat Commun. 2014 Jun 27;5:4217. doi: 10.1038/ncomms5217. PMID:24969970<ref>PMID:24969970</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 09:16, 9 July 2014
Solution structure of SUMO dimer in complex with SIM2-3 from RNF4Solution structure of SUMO dimer in complex with SIM2-3 from RNF4
Structural highlights
Publication Abstract from PubMedThe small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which targets substrates for proteasomal degradation. Here we use a segmental labelling approach combined with solution nuclear magnetic resonance (NMR) spectroscopy and biochemical characterization to reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer. Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4.,Xu Y, Plechanovova A, Simpson P, Marchant J, Leidecker O, Kraatz S, Hay RT, Matthews SJ Nat Commun. 2014 Jun 27;5:4217. doi: 10.1038/ncomms5217. PMID:24969970[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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