5suy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:33, 6 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Domain-swapped dimer of human Dishevelled2 DEP domain: monoclinic crystal form crystallised from dimeric fraction==
==Domain-swapped dimer of human Dishevelled2 DEP domain: monoclinic crystal form crystallised from dimeric fraction==
-
<StructureSection load='5suy' size='340' side='right' caption='[[5suy]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
+
<StructureSection load='5suy' size='340' side='right'caption='[[5suy]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5suy]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SUY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SUY FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5suy]] is a 4 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=5SUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SUY FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88&#8491;</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=5suy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5suy OCA], [http://pdbe.org/5suy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5suy RCSB], [http://www.ebi.ac.uk/pdbsum/5suy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5suy ProSAT]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5suy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5suy OCA], [https://pdbe.org/5suy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5suy RCSB], [https://www.ebi.ac.uk/pdbsum/5suy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5suy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://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>
+
[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 5suy" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Bienz, M]]
+
[[Category: Homo sapiens]]
-
[[Category: Gammons, M V]]
+
[[Category: Large Structures]]
-
[[Category: Renko, M]]
+
[[Category: Bienz M]]
-
[[Category: Dep domain]]
+
[[Category: Gammons MV]]
-
[[Category: Dishevelled]]
+
[[Category: Renko M]]
-
[[Category: Signaling protein]]
+
-
[[Category: Wnt signalling]]
+

Current revision

Domain-swapped dimer of human Dishevelled2 DEP domain: monoclinic crystal form crystallised from dimeric fraction

PDB ID 5suy

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5suy"
Personal tools