5ghb: Difference between revisions

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'''Unreleased structure'''


The entry 5ghb is ON HOLD  until Jun 19 2018
==SOLUTION STRUCTURE OF LYS42 ACETYLATED HUMAN SUMO2==
<StructureSection load='5ghb' size='340' side='right'caption='[[5ghb]]' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[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>


Authors: Naik, M.T., Naik, N., Shih, H., Huang, T.
==See Also==
 
*[[SUMO 3D Structures|SUMO 3D Structures]]
Description: SOLUTION STRUCTURE OF LYS42 ACETYLATED HUMAN SUMO2
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Huang, T]]
__TOC__
[[Category: Shih, H]]
</StructureSection>
[[Category: Naik, M.T]]
[[Category: Homo sapiens]]
[[Category: Naik, N]]
[[Category: Large Structures]]
[[Category: Huang T]]
[[Category: Naik MT]]
[[Category: Naik N]]
[[Category: Shih H]]