2n1w: Difference between revisions

Revision as of 21:37, 12 May 2016

Solution structure of human SUMO2Solution structure of human SUMO2

Structural highlights

2n1w is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1wm3, 2n1v, 2n1x, 2n1y, 2n1z, 2n20
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3]

References

↑ Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ET. Characterization of a second member of the sentrin family of ubiquitin-like proteins. J Biol Chem. 1998 May 1;273(18):11349-53. PMID:9556629
↑ Meulmeester E, Kunze M, Hsiao HH, Urlaub H, Melchior F. Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol Cell. 2008 Jun 6;30(5):610-9. doi: 10.1016/j.molcel.2008.03.021. PMID:18538659 doi:10.1016/j.molcel.2008.03.021
↑ Tatham MH, Geoffroy MC, Shen L, Plechanovova A, Hattersley N, Jaffray EG, Palvimo JJ, Hay RT. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol. 2008 May;10(5):538-46. doi: 10.1038/ncb1716. Epub 2008 Apr 13. PMID:18408734 doi:10.1038/ncb1716

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OCA

[1] Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ET. Characterization of a second member of the sentrin family of ubiquitin-like proteins. J Biol Chem. 1998 May 1;273(18):11349-53. PMID:9556629

[2] Meulmeester E, Kunze M, Hsiao HH, Urlaub H, Melchior F. Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol Cell. 2008 Jun 6;30(5):610-9. doi: 10.1016/j.molcel.2008.03.021. PMID:18538659 doi:10.1016/j.molcel.2008.03.021

[3] Tatham MH, Geoffroy MC, Shen L, Plechanovova A, Hattersley N, Jaffray EG, Palvimo JJ, Hay RT. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol. 2008 May;10(5):538-46. doi: 10.1038/ncb1716. Epub 2008 Apr 13. PMID:18408734 doi:10.1038/ncb1716

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[2]

[3]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2n1w is ON HOLD  until Apr 24 2017
+==Solution structure of human SUMO2==
+<StructureSection load='2n1w' size='340' side='right' caption='[[2n1w]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
-Authors: Naik, M.T., Naik, N., Shih, H., Huang, T.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2n1w]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N1W FirstGlance]. <br>
-Description: Solution structure of human SUMO2
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wm3|1wm3]], [[2n1v|2n1v]], [[2n1x|2n1x]], [[2n1y|2n1y]], [[2n1z|2n1z]], [[2n20|2n20]]</td></tr>
-[[Category: Unreleased Structures]]
+<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=2n1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1w OCA], [http://pdbe.org/2n1w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n1w RCSB], [http://www.ebi.ac.uk/pdbsum/2n1w PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Huang, T]]
+[[Category: Naik, M T]]
+[[Category: Naik, N]]
 [[Category: Shih, H]]
-[[Category: Naik, M.T]]
+[[Category: Structural genomic]]
-[[Category: Naik, N]]
+[[Category: Ubiquitin-like protein]]

2n1w: Difference between revisions

Revision as of 21:37, 12 May 2016

Solution structure of human SUMO2Solution structure of human SUMO2

Structural highlights

Function

References

Contents

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2n1w: Difference between revisions

Revision as of 21:37, 12 May 2016

Solution structure of human SUMO2Solution structure of human SUMO2

Structural highlights

Function

References

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