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2rpq
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:2rpq.png|left|200px]] | ||
| - | + | ==Solution Structure of a SUMO-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3== | |
| - | + | <StructureSection load='2rpq' size='340' side='right'caption='[[2rpq]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | or the | + | <table><tr><td colspan='2'>[[2rpq]] is a 2 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=2RPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RPQ FirstGlance]. <br> |
| - | or | + | </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=2rpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rpq OCA], [https://pdbe.org/2rpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rpq RCSB], [https://www.ebi.ac.uk/pdbsum/2rpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rpq ProSAT]</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/rp/2rpq_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=2rpq 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: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Ariyoshi M]] |
| - | [[Category: | + | [[Category: Baba D]] |
| - | [[Category: | + | [[Category: Ikegami T]] |
| - | [[Category: | + | [[Category: Ikeguchi M]] |
| - | [[Category: | + | [[Category: Saitoh H]] |
| - | [[Category: | + | [[Category: Sekiyama N]] |
| - | [[Category: | + | [[Category: Shirakawa M]] |
| - | [[Category: | + | [[Category: Tochio H]] |
| - | [[Category: | + | [[Category: Uchimura Y]] |
| - | [[Category: | + | [[Category: Yamane T]] |
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Current revision
Solution Structure of a SUMO-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3
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Categories: Homo sapiens | Large Structures | Ariyoshi M | Baba D | Ikegami T | Ikeguchi M | Saitoh H | Sekiyama N | Shirakawa M | Tochio H | Uchimura Y | Yamane T

