View source for 5suz


==Domain-swapped dimer of human Dishevelled2 DEP domain: C-centered monoclinic crystal form crystallised from monomeric fraction==
<StructureSection load='5suz' size='340' side='right'caption='[[5suz]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5suz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SUZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5suz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5suz OCA], [https://pdbe.org/5suz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5suz RCSB], [https://www.ebi.ac.uk/pdbsum/5suz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5suz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DVL2_HUMAN DVL2_HUMAN] Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes (By similarity).<ref>PMID:19252499</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Extracellular signals are often transduced by dynamic signaling complexes ("signalosomes") assembled by oligomerizing hub proteins following their recruitment to signal-activated transmembrane receptors. A paradigm is the Wnt signalosome, which is assembled by Dishevelled via reversible head-to-tail polymerization by its DIX domain. Its activity causes stabilization of beta-catenin, a Wnt effector with pivotal roles in animal development and cancer. How Wnt triggers signalosome assembly is unknown. Here, we use structural analysis, as well as biophysical and cell-based assays, to show that the DEP domain of Dishevelled undergoes a conformational switch, from monomeric to swapped dimer, to trigger DIX-dependent polymerization and signaling to beta-catenin. This occurs in two steps: binding of monomeric DEP to Frizzled followed by DEP domain swapping triggered by its high local concentration upon Wnt-induced recruitment into clathrin-coated pits. DEP domain swapping confers directional bias on signaling, and the dimerization provides cross-linking between Dishevelled polymers, illustrating a key principle underlying signalosome formation.

Wnt Signalosome Assembly by DEP Domain Swapping of Dishevelled.,Gammons MV, Renko M, Johnson CM, Rutherford TJ, Bienz M Mol Cell. 2016 Oct 6;64(1):92-104. doi: 10.1016/j.molcel.2016.08.026. Epub 2016, Sep 29. PMID:27692984<ref>PMID:27692984</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5suz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bienz M]]
[[Category: Gammons MV]]
[[Category: Renko M]]