4bkg: Difference between revisions

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{{STRUCTURE_4bkg|  PDB=4bkg | SCENE= }}
==crystal structure of human diSUMO-2==
===crystal structure of human diSUMO-2===
<StructureSection load='4bkg' size='340' side='right' caption='[[4bkg]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
{{ABSTRACT_PUBMED_24151981}}
== 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>
</table>
<div style="background-color:#fffaf0;">
== 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.


==Function==
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>
[[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>


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[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].
</div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:024151981</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Bade, V N.]]
[[Category: Bade, V N]]
[[Category: Dohmen, R J.]]
[[Category: Dohmen, R J]]
[[Category: Fischer-Schrader, K.]]
[[Category: Fischer-Schrader, K]]
[[Category: Hofmann, K.]]
[[Category: Hofmann, K]]
[[Category: Horst, C.]]
[[Category: Horst, C]]
[[Category: Keusekotten, K.]]
[[Category: Keusekotten, K]]
[[Category: Krause, A.]]
[[Category: Krause, A]]
[[Category: Meyer-Teschendorf, K.]]
[[Category: Meyer-Teschendorf, K]]
[[Category: Praefcke, G J.K.]]
[[Category: Praefcke, G J.K]]
[[Category: Sriramachandran, A.]]
[[Category: Sriramachandran, A]]
[[Category: Protein binding]]
[[Category: Protein binding]]

Revision as of 16:56, 21 December 2014

crystal structure of human diSUMO-2

4bkg, resolution 2.11Å

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