3zo5

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==Structure of SENP2-Loop1 in complex with preSUMO-2==
==Structure of SENP2-Loop1 in complex with preSUMO-2==
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<StructureSection load='3zo5' size='340' side='right' caption='[[3zo5]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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<StructureSection load='3zo5' size='340' side='right'caption='[[3zo5]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3zo5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZO5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3zo5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZO5 FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ulp1_peptidase Ulp1 peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.68 3.4.22.68] </span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<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=3zo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zo5 OCA], [http://pdbe.org/3zo5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zo5 RCSB], [http://www.ebi.ac.uk/pdbsum/3zo5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zo5 ProSAT]</span></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=3zo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zo5 OCA], [https://pdbe.org/3zo5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zo5 RCSB], [https://www.ebi.ac.uk/pdbsum/3zo5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zo5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SENP2_HUMAN 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).<ref>PMID:12192048</ref> <ref>PMID:11896061</ref> [[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>
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[https://www.uniprot.org/uniprot/SENP2_HUMAN 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).<ref>PMID:12192048</ref> <ref>PMID:11896061</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[SUMO|SUMO]]
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*[[SUMO 3D Structures|SUMO 3D Structures]]
*[[Sentrin-specific protease|Sentrin-specific protease]]
*[[Sentrin-specific protease|Sentrin-specific protease]]
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Ulp1 peptidase]]
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[[Category: Large Structures]]
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[[Category: Alegre, K O]]
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[[Category: Alegre KO]]
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[[Category: Reverter, D]]
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[[Category: Reverter D]]
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[[Category: Hydrolase-signaling protein complex]]
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Current revision

Structure of SENP2-Loop1 in complex with preSUMO-2

PDB ID 3zo5

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