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[[Image:1wz0.gif|left|200px]]<br /><applet load="1wz0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1wz0" />
'''Solution Structure of Human SUMO-2 (SMT3B), a Ubiquitin-like Protein'''<br />


==About this Structure==
==Solution Structure of Human SUMO-2 (SMT3B), a Ubiquitin-like Protein==
1WZ0 is a [http://en.wikipedia.org/wiki/Single_protein 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=1WZ0 OCA].  
<StructureSection load='1wz0' size='340' side='right'caption='[[1wz0]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wz0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZ0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wz0 OCA], [https://pdbe.org/1wz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wz0 RCSB], [https://www.ebi.ac.uk/pdbsum/1wz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wz0 ProSAT], [https://www.topsan.org/Proteins/RSGI/1wz0 TOPSAN]</span></td></tr>
</table>
== Function ==
[https://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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wz/1wz0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1wz0 ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[SUMO 3D Structures|SUMO 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Inoue, M.]]
[[Category: Inoue M]]
[[Category: Kigawa, T.]]
[[Category: Kigawa T]]
[[Category: Koshiba, S.]]
[[Category: Koshiba S]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Saito K]]
[[Category: Saito, K.]]
[[Category: Yokoyama S]]
[[Category: Yokoyama, S.]]
[[Category: Zhao C]]
[[Category: Zhao, C.]]
[[Category: nppfsa]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: sentrin2]]
[[Category: structural genomics]]
[[Category: sumo-2]]
[[Category: ubiquitin-like molecule]]
 
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