5y3b

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(New page: ==Crystal structure of mouse Ccd1 DIX domain== <StructureSection load='5y3b' size='340' side='right' caption='5y3b, resolution 3.00&Aring;' scene=''> == Structural high...)
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==Crystal structure of mouse Ccd1 DIX domain==
==Crystal structure of mouse Ccd1 DIX domain==
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<StructureSection load='5y3b' size='340' side='right' caption='[[5y3b]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='5y3b' size='340' side='right'caption='[[5y3b]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5y3b]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y3B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y3B FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5y3b]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y3B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y3B FirstGlance]. <br>
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</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=5y3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y3b OCA], [http://pdbe.org/5y3b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y3b RCSB], [http://www.ebi.ac.uk/pdbsum/5y3b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y3b ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5y3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y3b OCA], [https://pdbe.org/5y3b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y3b RCSB], [https://www.ebi.ac.uk/pdbsum/5y3b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y3b ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DIXC1_MOUSE DIXC1_MOUSE]] Positive effector of the Wnt signaling pathway; activates WNT3A signaling via DVL2. Regulates JNK activation by AXIN1 and DVL2.<ref>PMID:15262978</ref> <ref>PMID:15857680</ref>
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[https://www.uniprot.org/uniprot/DIXC1_MOUSE DIXC1_MOUSE] Positive effector of the Wnt signaling pathway; activates WNT3A signaling via DVL2. Regulates JNK activation by AXIN1 and DVL2.<ref>PMID:15262978</ref> <ref>PMID:15857680</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Wnt signaling plays an important role in governing cell fate decisions. Coiled-coil-DIX1 (Ccd1), Dishevelled (Dvl), and Axin are signaling proteins that regulate the canonical pathway by controlling the stability of a key signal transducer beta-catenin. These proteins contain the DIX domain with a ubiquitin-like fold, which mediates their interaction in the beta-catenin destruction complex through dynamic head-to-tail polymerization. Despite high sequence similarities, mammalian Ccd1 shows weaker stimulation of beta-catenin transcriptional activity compared with zebrafish (z) Ccd1 in cultured cells. Here, we show that the mouse (m) Ccd1 DIX domain displays weaker ability for homopolymerization than that of zCcd1. Furthermore, X-ray crystallographic analysis of mCcd1 and zCcd1 DIX domains revealed that mCcd1 was assembled into a double-helical filament by the insertion of the beta1-beta2 loop into the head-to-tail interface, whereas zCcd1 formed a typical single-helical polymer similar to Dvl1 and Axin. The mutation in the contact interface of mCcd1 double-helical polymer changed the hydrodynamic properties of mCcd1 so that it acquired the ability to induce Wnt-specific transcriptional activity similar to zCcd1. These findings suggest a novel regulatory mechanism by which mCcd1 modulates Wnt signaling through auto-inhibition of dynamic head-to-tail homopolymerization.
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Structural basis for Ccd1 auto-inhibition in the Wnt pathway through homomerization of the DIX domain.,Terawaki SI, Fujita S, Katsutani T, Shiomi K, Keino-Masu K, Masu M, Wakamatsu K, Shibata N, Higuchi Y Sci Rep. 2017 Aug 10;7(1):7739. doi: 10.1038/s41598-017-08019-5. PMID:28798413<ref>PMID:28798413</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5y3b" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Higuchi, Y]]
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[[Category: Large Structures]]
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[[Category: Shibata, N]]
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[[Category: Mus musculus]]
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[[Category: Terawaki, S]]
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[[Category: Higuchi Y]]
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[[Category: Signaling protein]]
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[[Category: Shibata N]]
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[[Category: Wnt signal]]
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[[Category: Terawaki S]]

Current revision

Crystal structure of mouse Ccd1 DIX domain

PDB ID 5y3b

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