View source for 6iw3


==High resolution structure of Dvl2-DIX Y27W/C80S mutant==
<StructureSection load='6iw3' size='340' side='right'caption='[[6iw3]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6iw3]] is a 1 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=6IW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IW3 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]] 1.64&#8491;</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=6iw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iw3 OCA], [https://pdbe.org/6iw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iw3 RCSB], [https://www.ebi.ac.uk/pdbsum/6iw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iw3 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 ==
Dishevelled (Dvl) is a positive regulator of the canonical Wnt pathway that downregulates the phosphorylation of beta-catenin and its subsequent degradation. Dvl contains an N-terminal DIX domain, which is involved in its homooligomerization and interactions with regulators of the Wnt pathway. The crystal structure of a Y27W mutant of the Dishevelled2 DIX domain (DIX-Y27W) has been determined at 1.64 A resolution. DIX-Y27W has a compact ubiquitin-like fold and self-associates with neighbouring molecules through beta-bridges, resulting in a head-to-tail helical molecular arrangement similar to previously reported structures of DIX domains. Glu23 of DIX-Y27W forms a hydrogen bond to the side chain of Trp27, corresponding to the Glu762...Trp766 hydrogen bond of the rat Axin DIX domain, whereas Glu23 in the Y27D mutant of the Dishevelled2 DIX domain forms a salt bridge to Lys68 of the adjacent molecule. The high-resolution DIX-Y27W structure provides details of the head-to-tail interaction, including solvent molecules, and also the plausibly wild-type-like structure of the self-association surface compared with previously published Dvl DIX-domain mutants.

High-resolution structure of a Y27W mutant of the Dishevelled2 DIX domain.,Yamanishi K, Sin Y, Terawaki SI, Higuchi Y, Shibata N Acta Crystallogr F Struct Biol Commun. 2019 Feb 1;75(Pt 2):116-122. doi:, 10.1107/S2053230X18018290. Epub 2019 Jan 23. PMID:30713163<ref>PMID:30713163</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6iw3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Shibata N]]
[[Category: Yamanishi K]]