4bkg

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'''Unreleased structure'''
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{{STRUCTURE_4bkg| PDB=4bkg | SCENE= }}
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===crystal structure of human diSUMO-2===
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{{ABSTRACT_PUBMED_24151981}}
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The entry 4bkg is ON HOLD until Paper Publication
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==Function==
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[[http://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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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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==About this Structure==
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[[4bkg]] is a 1 chain structure with 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=4BKG OCA].
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Description: crystal structure of human diSUMO-2
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==Reference==
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<ref group="xtra">PMID:024151981</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Bade, V N.]]
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[[Category: Dohmen, R J.]]
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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, G J.K.]]
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[[Category: Sriramachandran, A.]]
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[[Category: Protein binding]]

Revision as of 07:37, 6 November 2013

Template:STRUCTURE 4bkg

Contents

crystal structure of human diSUMO-2

Template:ABSTRACT PUBMED 24151981

Function

[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.[1] [2] [3]

About this Structure

4bkg is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Keusekotten K, Bade VN, Meyer-Teschendorf K, Sriramachandran AM, Fischer-Schrader K, Krause A, Horst C, Schwarz G, Hofmann K, Dohmen RJ, Praefcke GJ. 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). Biochem J. 2013 Oct 23. PMID:24151981 doi:http://dx.doi.org/10.1042/BJ20130753
  1. ↑ Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ET. Characterization of a second member of the sentrin family of ubiquitin-like proteins. J Biol Chem. 1998 May 1;273(18):11349-53. PMID:9556629
  2. ↑ Meulmeester E, Kunze M, Hsiao HH, Urlaub H, Melchior F. Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol Cell. 2008 Jun 6;30(5):610-9. doi: 10.1016/j.molcel.2008.03.021. PMID:18538659 doi:10.1016/j.molcel.2008.03.021
  3. ↑ Tatham MH, Geoffroy MC, Shen L, Plechanovova A, Hattersley N, Jaffray EG, Palvimo JJ, Hay RT. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol. 2008 May;10(5):538-46. doi: 10.1038/ncb1716. Epub 2008 Apr 13. PMID:18408734 doi:10.1038/ncb1716

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