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4bkg

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Current revision (11:53, 20 December 2023) (edit) (undo)
 
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<StructureSection load='4bkg' size='340' side='right'caption='[[4bkg]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
<StructureSection load='4bkg' size='340' side='right'caption='[[4bkg]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4bkg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BKG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4bkg]] is a 1 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=4BKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BKG FirstGlance]. <br>
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</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=4bkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bkg OCA], [https://pdbe.org/4bkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bkg RCSB], [https://www.ebi.ac.uk/pdbsum/4bkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bkg ProSAT]</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]] 2.11&#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=4bkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bkg OCA], [https://pdbe.org/4bkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bkg RCSB], [https://www.ebi.ac.uk/pdbsum/4bkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bkg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bade, V N]]
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[[Category: Bade VN]]
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[[Category: Dohmen, R J]]
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[[Category: Dohmen RJ]]
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[[Category: Fischer-Schrader, K]]
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[[Category: Fischer-Schrader K]]
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[[Category: Hofmann, K]]
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[[Category: Hofmann K]]
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[[Category: Horst, C]]
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[[Category: Horst C]]
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[[Category: Keusekotten, K]]
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[[Category: Keusekotten K]]
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[[Category: Krause, A]]
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[[Category: Krause A]]
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[[Category: Meyer-Teschendorf, K]]
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[[Category: Meyer-Teschendorf K]]
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[[Category: Praefcke, G J.K]]
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[[Category: Praefcke GJK]]
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[[Category: Sriramachandran, A]]
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[[Category: Sriramachandran A]]
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[[Category: Protein binding]]
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Current revision

crystal structure of human diSUMO-2

PDB ID 4bkg

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