1th0

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{{Seed}}
 
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[[Image:1th0.png|left|200px]]
 
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==Structure of human Senp2==
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The line below this paragraph, containing "STRUCTURE_1th0", creates the "Structure Box" on the page.
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<StructureSection load='1th0' size='340' side='right'caption='[[1th0]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1th0]] 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=1TH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TH0 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.2&#8491;</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=1th0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1th0 OCA], [https://pdbe.org/1th0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1th0 RCSB], [https://www.ebi.ac.uk/pdbsum/1th0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1th0 ProSAT]</span></td></tr>
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{{STRUCTURE_1th0| PDB=1th0 | SCENE= }}
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</table>
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== Function ==
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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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/th/1th0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1th0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear metabolism and cell cycle progression in yeast. X-ray structures of the human Senp2 catalytic protease domain and of a covalent thiohemiacetal transition-state complex obtained between the Senp2 catalytic domain and SUMO-1 revealed details of the respective protease and substrate surfaces utilized in interactions between these two proteins. Comparative biochemical and structural analysis between Senp2 and the yeast SUMO protease Ulp1 revealed differential abilities to process SUMO-1, SUMO-2, and SUMO-3 in maturation and deconjugation reactions. Further biochemical characterization of the three SUMO isoforms into which an additional Gly-Gly di-peptide was inserted, or whereby the respective SUMO tails from the three isoforms were swapped, suggests a strict dependence for SUMO isopeptidase activity on residues C-terminal to the conserved Gly-Gly motif and preferred cleavage site for SUMO proteases.
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===Structure of human Senp2===
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A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex.,Reverter D, Lima CD Structure. 2004 Aug;12(8):1519-31. PMID:15296745<ref>PMID:15296745</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1th0" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15296745}}, adds the Publication Abstract to the page
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*[[Sentrin-specific protease|Sentrin-specific protease]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15296745 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15296745}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1TH0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TH0 OCA].
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==Reference==
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A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex., Reverter D, Lima CD, Structure. 2004 Aug;12(8):1519-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15296745 15296745]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Lima, C D.]]
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[[Category: Lima CD]]
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[[Category: Reverter, D.]]
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[[Category: Reverter D]]
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[[Category: Axam]]
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[[Category: Protease]]
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[[Category: Senp]]
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[[Category: Sumo]]
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[[Category: Ulp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:26:53 2008''
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Current revision

Structure of human Senp2

PDB ID 1th0

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