5ghb

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(New page: '''Unreleased structure''' The entry 5ghb is ON HOLD until Jun 19 2018 Authors: Naik, M.T., Naik, N., Shih, H., Huang, T. Description: SOLUTION STRUCTURE OF LYS42 ACETYLATED HUMAN SUMO...)
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'''Unreleased structure'''
 
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The entry 5ghb is ON HOLD until Jun 19 2018
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==SOLUTION STRUCTURE OF LYS42 ACETYLATED HUMAN SUMO2==
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<StructureSection load='5ghb' size='340' side='right'caption='[[5ghb]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ghb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GHB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GHB 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, 20 models</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></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=5ghb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ghb OCA], [https://pdbe.org/5ghb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ghb RCSB], [https://www.ebi.ac.uk/pdbsum/5ghb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ghb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SUMO2_HUMAN SUMO2_HUMAN] Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond 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. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins.<ref>PMID:9556629</ref> <ref>PMID:18538659</ref> <ref>PMID:18408734</ref>
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Authors: Naik, M.T., Naik, N., Shih, H., Huang, T.
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==See Also==
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*[[SUMO 3D Structures|SUMO 3D Structures]]
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Description: SOLUTION STRUCTURE OF LYS42 ACETYLATED HUMAN SUMO2
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Huang, T]]
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__TOC__
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[[Category: Naik, M.T]]
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</StructureSection>
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[[Category: Naik, N]]
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[[Category: Homo sapiens]]
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[[Category: Shih, H]]
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[[Category: Large Structures]]
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[[Category: Huang T]]
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[[Category: Naik MT]]
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[[Category: Naik N]]
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[[Category: Shih H]]

Current revision

SOLUTION STRUCTURE OF LYS42 ACETYLATED HUMAN SUMO2

PDB ID 5ghb

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