4npn
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ''' | + | ==Crystal structure of human tetra-SUMO-2== |
| + | <StructureSection load='4npn' size='340' side='right' caption='[[4npn]], [[Resolution|resolution]] 1.63Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4npn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NPN FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bkg|4bkg]], [[1wm2|1wm2]], [[1wm3|1wm3]], [[2rpq|2rpq]]</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=4npn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4npn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4npn RCSB], [http://www.ebi.ac.uk/pdbsum/4npn PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The E3 ubiquitin ligase RNF4 (RING finger protein 4) contains four tandem SIM [SUMO (small ubiquitin-like modifier)-interaction motif] repeats for selective interaction with poly-SUMO-modified proteins, which it targets for degradation. We employed a multi-faceted approach to characterize the structure of the RNF4-SIMs domain and the tetra-SUMO2 chain to elucidate the interaction between them. In solution, the SIM domain was intrinsically disordered and the linkers of the tetra-SUMO2 were highly flexible. Individual SIMs of the RNF4-SIMs domains bind to SUMO2 in the groove between the beta2-strand and the alpha1-helix parallel to the beta2-strand. SIM2 and SIM3 bound to SUMO with a high affinity and together constituted the recognition module necessary for SUMO binding. SIM4 alone bound to SUMO with low affinity; however, its contribution to tetra-SUMO2 binding avidity is comparable with that of SIM3 when in the RNF4-SIMs domain. The SAXS data of the tetra-SUMO2-RNF4-SIMs domain complex indicate that it exists as an ordered structure. The HADDOCK model showed that the tandem RNF4-SIMs domain bound antiparallel to the tetra-SUMO2 chain orientation and wrapped around the SUMO protamers in a superhelical turn without imposing steric hindrance on either molecule. | ||
| - | + | Structural analysis of poly-SUMO chain recognition by the RNF4-SIMs domain.,Kung CC, Naik MT, Wang SH, Shih HM, Chang CC, Lin LY, Chen CL, Ma C, Chang CF, Huang TH Biochem J. 2014 Aug 15;462(1):53-65. doi: 10.1042/BJ20140521. PMID:24844634<ref>PMID:24844634</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chen, C L.]] | ||
| + | [[Category: Huang, T H.]] | ||
| + | [[Category: Kung, C C.H.]] | ||
| + | [[Category: Ma, C.]] | ||
| + | [[Category: Naik, M T.]] | ||
| + | [[Category: Protein binding]] | ||
| + | [[Category: Protein transport]] | ||
Revision as of 10:44, 20 October 2014
Crystal structure of human tetra-SUMO-2
| |||||||||||
