4npn: Difference between revisions

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-'''Unreleased structure'''
+==Crystal structure of human tetra-SUMO-2==
+<StructureSection load='4npn' size='340' side='right' caption='[[4npn]], [[Resolution|resolution]] 1.63&Aring;' 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.
-The entry 4npn is ON HOLD  until Paper Publication
+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>
-Authors: Kung, C.C.-H., Naik, M.T., Chen, C.L., Ma, C., Huang, T.H.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of human tetra-SUMO-2
+== 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]]