2n1w: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 2n1w is ~~ON HOLD~~

==Solution structure of human SUMO2==

== Structural highlights ==

<table><tr><td colspan='2'>[[2n1w]] 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=2N1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N1W FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2n1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1w OCA], [https://pdbe.org/2n1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n1w RCSB], [https://www.ebi.ac.uk/pdbsum/2n1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1w 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 human SUMO2~~

== References ==

[[Category: ~~Unreleased~~ Structures]]

[[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]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2n1w is ON HOLD
+==Solution structure of human SUMO2==
+<StructureSection load='2n1w' size='340' side='right'caption='[[2n1w]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2n1w]] 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=2N1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N1W FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2n1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1w OCA], [https://pdbe.org/2n1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n1w RCSB], [https://www.ebi.ac.uk/pdbsum/2n1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1w 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 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]]