2ckh

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[[Image:2ckh.gif|left|200px]]
 
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{{Structure
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==SENP1-SUMO2 complex==
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|PDB= 2ckh |SIZE=350|CAPTION= <scene name='initialview01'>2ckh</scene>, resolution 3.20&Aring;
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<StructureSection load='2ckh' size='340' side='right'caption='[[2ckh]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2ckh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bzo 2bzo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CKH FirstGlance]. <br>
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|ACTIVITY=
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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]] 3.2&#8491;</td></tr>
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|GENE=
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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=2ckh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckh OCA], [https://pdbe.org/2ckh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ckh RCSB], [https://www.ebi.ac.uk/pdbsum/2ckh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ckh ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ckh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckh OCA], [http://www.ebi.ac.uk/pdbsum/2ckh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ckh RCSB]</span>
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[https://www.uniprot.org/uniprot/SENP1_HUMAN SENP1_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. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1, which decreases its transcriptional repression activity.<ref>PMID:10652325</ref> <ref>PMID:15199155</ref> <ref>PMID:16253240</ref> <ref>PMID:16553580</ref>
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}}
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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/ck/2ckh_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=2ckh 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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The SUMO (small ubiquitin-like modifier)-specific protease SENP1 (sentrin-specific protease 1) can process the three forms of SUMO to their mature forms and deconjugate SUMO from modified substrates. It has been demonstrated previously that SENP1 processed SUMO-1 more efficiently than SUMO-2, but displayed little difference in its ability to deconjugate the different SUMO paralogues from modified substrates. To determine the basis for this substrate specificity, we have determined the crystal structure of SENP1 in isolation and in a transition-state complex with SUMO-2. The interface between SUMO-2 and SENP1 has a relatively poor complementarity, and most of the recognition is determined by interaction between the conserved C-terminus of SUMO-2 and the cleft in the protease. Although SENP1 is rather similar in structure to the related protease SENP2, these proteases have different SUMO-processing activities. Electrostatic analysis of SENP1 in the region where the C-terminal peptide, removed during maturation, would project indicates that it is the electrostatic complementarity between this region of SENP1 and the C-terminal peptides of the various SUMO paralogues that mediates selectivity.
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'''SENP1-SUMO2 COMPLEX'''
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The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing.,Shen LN, Dong C, Liu H, Naismith JH, Hay RT Biochem J. 2006 Jul 15;397(2):279-88. PMID:16553580<ref>PMID:16553580</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 2ckh" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The SUMO (small ubiquitin-like modifier)-specific protease SENP1 (sentrin-specific protease 1) can process the three forms of SUMO to their mature forms and deconjugate SUMO from modified substrates. It has been demonstrated previously that SENP1 processed SUMO-1 more efficiently than SUMO-2, but displayed little difference in its ability to deconjugate the different SUMO paralogues from modified substrates. To determine the basis for this substrate specificity, we have determined the crystal structure of SENP1 in isolation and in a transition-state complex with SUMO-2. The interface between SUMO-2 and SENP1 has a relatively poor complementarity, and most of the recognition is determined by interaction between the conserved C-terminus of SUMO-2 and the cleft in the protease. Although SENP1 is rather similar in structure to the related protease SENP2, these proteases have different SUMO-processing activities. Electrostatic analysis of SENP1 in the region where the C-terminal peptide, removed during maturation, would project indicates that it is the electrostatic complementarity between this region of SENP1 and the C-terminal peptides of the various SUMO paralogues that mediates selectivity.
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*[[SUMO 3D Structures|SUMO 3D Structures]]
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*[[Sentrin-specific protease|Sentrin-specific protease]]
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==About this Structure==
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== References ==
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2CKH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 2BZO. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKH OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing., Shen LN, Dong C, Liu H, Naismith JH, Hay RT, Biochem J. 2006 Jul 15;397(2):279-88. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16553580 16553580]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Dong, C.]]
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[[Category: Dong C]]
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[[Category: Hay, R T.]]
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[[Category: Hay RT]]
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[[Category: Liu, H.]]
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[[Category: Liu H]]
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[[Category: Naismith, J H.]]
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[[Category: Naismith JH]]
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[[Category: Shen, L.]]
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[[Category: Shen LN]]
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[[Category: hydrolase]]
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[[Category: nuclear protein]]
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[[Category: protease]]
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[[Category: protease co-complex]]
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[[Category: sumo]]
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[[Category: thiol protease]]
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[[Category: ubl conjugation pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:22:44 2008''
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Current revision

SENP1-SUMO2 complex

PDB ID 2ckh

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