2mp2

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(New page: '''Unreleased structure''' The entry 2mp2 is ON HOLD Authors: Xu, Y., Plechanovov, A., Simpson, P., Marchant, J., Leidecker, O., Sebastian, K., Hay, R.T., Matthews, S.J. Description: S...)
Current revision (07:01, 1 May 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2mp2 is ON HOLD
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==Solution structure of SUMO dimer in complex with SIM2-3 from RNF4==
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<StructureSection load='2mp2' size='340' side='right'caption='[[2mp2]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2mp2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2MP2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mp2 OCA], [https://pdbe.org/2mp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mp2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mp2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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>
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Authors: Xu, Y., Plechanovov, A., Simpson, P., Marchant, J., Leidecker, O., Sebastian, K., Hay, R.T., Matthews, S.J.
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==See Also==
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*[[SUMO 3D Structures|SUMO 3D Structures]]
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Description: Solution structure of SUMO dimer in complex with SIM2-3 from RNF4
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Hay RT]]
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[[Category: Leidecker O]]
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[[Category: Marchant J]]
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[[Category: Matthews SJ]]
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[[Category: Plechanovov A]]
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[[Category: Sebastian K]]
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[[Category: Simpson P]]
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[[Category: Xu Y]]

Current revision

Solution structure of SUMO dimer in complex with SIM2-3 from RNF4

PDB ID 2mp2

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