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4bkg

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Revision as of 07:49, 4 August 2016

crystal structure of human diSUMO-2

Structural highlights

4bkg is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ 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
↑ 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 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4bkg"

@@ Line 1: / Line 1: @@
 ==crystal structure of human diSUMO-2==
 <StructureSection load='4bkg' size='340' side='right' caption='[[4bkg]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4bkg]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BKG FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bkg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bkg RCSB], [http://www.ebi.ac.uk/pdbsum/4bkg PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bkg OCA], [http://pdbe.org/4bkg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bkg RCSB], [http://www.ebi.ac.uk/pdbsum/4bkg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bkg ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4bkg" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[SUMO|SUMO]]
 == References ==
 <references/>

4bkg

From Proteopedia

Revision as of 07:49, 4 August 2016

crystal structure of human diSUMO-2

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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