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4bkg

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'''Unreleased structure'''
 
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The entry 4bkg is ON HOLD until sometime in the future
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==crystal structure of human diSUMO-2==
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<StructureSection load='4bkg' size='340' side='right'caption='[[4bkg]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
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== 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/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='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>
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</table>
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== 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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RNF4 [RING (really interesting new gene) finger protein 4] is a SUMO-targeted ubiquitin ligase (STUbL) controlling promyelocytic leukemia (PML) nuclear bodies, DNA double strand break repair and other nuclear functions. We describe that the sequence and spacing of the SUMO-interaction motifs (SIMs) in RNF4 regulate the avidity-driven recognition of substrate proteins carrying SUMO chains of variable length.
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Authors: Keusekotten, K., Bade, V.N., Meyer-Teschendorf, K., Sriramachandran, A., Fischer-Schrader, K., Krause, A., Horst, C., Hofmann, K., Dohmen, R.J., Praefcke, G.J.K.
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Multivalent interactions of the SUMO-interaction motifs in the RING-finger protein 4 (RNF4) determine the specificity for chains of the small ubiquitin-related modifier (SUMO).,Keusekotten K, Bade VN, Meyer-Teschendorf K, Sriramachandran AM, Fischer-Schrader K, Krause A, Horst C, Schwarz G, Hofmann K, Dohmen RJ, Praefcke GJ Biochem J. 2013 Oct 23. PMID:24151981<ref>PMID:24151981</ref>
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Description: crystal structure of human diSUMO-2
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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 4bkg" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[SUMO 3D Structures|SUMO 3D Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Bade VN]]
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[[Category: Dohmen RJ]]
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[[Category: Fischer-Schrader K]]
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[[Category: Hofmann K]]
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[[Category: Horst C]]
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[[Category: Keusekotten K]]
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[[Category: Krause A]]
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[[Category: Meyer-Teschendorf K]]
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[[Category: Praefcke GJK]]
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[[Category: Sriramachandran A]]

Current revision

crystal structure of human diSUMO-2

PDB ID 4bkg

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