2mp2: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mp2]] is a 3 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MP2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2mp2]] is a 3 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MP2 FirstGlance]. <br> | ||
</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 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=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> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/SUMO3_HUMAN SUMO3_HUMAN]] Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4.<ref>PMID:11451954</ref> <ref>PMID:18538659</ref> [[http://www.uniprot.org/uniprot/RNF4_MOUSE RNF4_MOUSE]] E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.<ref>PMID:20681948</ref> | |||
<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: Hay, R T | [[Category: Hay, R T]] | ||
[[Category: Leidecker, O | [[Category: Leidecker, O]] | ||
[[Category: Marchant, J | [[Category: Marchant, J]] | ||
[[Category: Matthews, S J | [[Category: Matthews, S J]] | ||
[[Category: Plechanovov, A | [[Category: Plechanovov, A]] | ||
[[Category: Sebastian, K | [[Category: Sebastian, K]] | ||
[[Category: Simpson, P | [[Category: Simpson, P]] | ||
[[Category: Xu, Y | [[Category: Xu, Y]] | ||
[[Category: Complex]] | [[Category: Complex]] | ||
[[Category: Dimer]] | [[Category: Dimer]] | ||
Revision as of 21:28, 24 December 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
Function[SUMO3_HUMAN] Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4.[1] [2] [RNF4_MOUSE] E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.[3] 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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