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3zo5
From Proteopedia
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{{STRUCTURE_3zo5| PDB=3zo5 | SCENE= }} | {{STRUCTURE_3zo5| PDB=3zo5 | SCENE= }} | ||
===Structure of SENP2-Loop1 in complex with preSUMO-2=== | ===Structure of SENP2-Loop1 in complex with preSUMO-2=== | ||
| + | {{ABSTRACT_PUBMED_24424631}} | ||
==Function== | ==Function== | ||
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==Reference== | ==Reference== | ||
| - | <references group="xtra"/><references/> | + | <ref group="xtra">PMID:024424631</ref><references group="xtra"/><references/> |
[[Category: Ulp1 peptidase]] | [[Category: Ulp1 peptidase]] | ||
[[Category: Alegre, K O.]] | [[Category: Alegre, K O.]] | ||
[[Category: Reverter, D.]] | [[Category: Reverter, D.]] | ||
[[Category: Hydrolase-signaling protein complex]] | [[Category: Hydrolase-signaling protein complex]] | ||
Revision as of 07:23, 2 April 2014
Contents |
Structure of SENP2-Loop1 in complex with preSUMO-2
Template:ABSTRACT PUBMED 24424631
Function
[SENP2_HUMAN] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway (By similarity).[1] [2] [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.[3] [4] [5]
About this Structure
3zo5 is a 2 chain structure. Full crystallographic information is available from OCA.
Reference
- Alegre KO, Reverter D. Structural insights into the SENP6 Loop1 structure in complex with SUMO2. Protein Sci. 2014 Apr;23(4):433-41. doi: 10.1002/pro.2425. Epub 2014 Mar 10. PMID:24424631 doi:http://dx.doi.org/10.1002/pro.2425
- ↑ Zhang H, Saitoh H, Matunis MJ. Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex. Mol Cell Biol. 2002 Sep;22(18):6498-508. PMID:12192048
- ↑ Hang J, Dasso M. Association of the human SUMO-1 protease SENP2 with the nuclear pore. J Biol Chem. 2002 May 31;277(22):19961-6. Epub 2002 Mar 14. PMID:11896061 doi:10.1074/jbc.M201799200
- ↑ 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
