3fy5
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3fy5 is ON HOLD Authors: Earnest, T., Friedland, N., Hung, L.-W., Moon, R. Description: Dishevelled PDZ domain homodimer ''Page seeded by [http://...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Dishevelled PDZ domain homodimer== | |
| - | + | <StructureSection load='3fy5' size='340' side='right'caption='[[3fy5]], [[Resolution|resolution]] 2.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3fy5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FY5 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]] 2.4Å</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=3fy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fy5 OCA], [https://pdbe.org/3fy5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fy5 RCSB], [https://www.ebi.ac.uk/pdbsum/3fy5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fy5 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DVL2_XENLA DVL2_XENLA] Involved in at least 2 independent signaling cascades, controlling cell fate via canonical Wnt signaling and cell polarity via a planar cell polarity (PCP) cascade. Acts synergistically with dal/dapple-like to activate Wnt signaling, stabilizing ctnnb1/beta-catenin and leading to dorsal axis formation. Also prevents degradation of ctnnb1/beta-catenin by displacing gsk3 from a complex with ARP/Axin-related protein. Has an additional role in anterior-posterior (A/P) axis formation, specifying different neuroectodermal cell fates along the A/P axis in a dose-dependent manner by activating several early patterning genes. In the PCP pathway, required at the cell membrane for PCP-mediated neural and mesodermal convergent extension during gastrulation and subsequent neural tube closure, acting to activate jnk. Also involved in blastopore closure and archenteron elongation during early, but not late, gastrulation. Associates with ephrin receptors and ligands and acts as part of a downstream PCP pathway to mediate ephrin-mediated cell repulsion via activation of rhoa. Required for efnb1/ephrin-B1-driven movement of non-retinal progenitor cells into the retina during eye field formation. Patterns the hindbrain. Required for ciliogenesis. Controls the docking of basal bodies to the apical plasma membrane; mediates the activation, but not localization of rhoa at the apical surface of ciliated cells during basal body docking. Furthermore, required for the association of basal bodies with membrane-bound vesicles and the vesicle-trafficking protein exoc4/sec8, and this association is in turn required for basal body docking. Once basal bodies are docked, required for the planar polarization of basal bodies that underlies ciliary beating and the directional fluid flow across ciliated epithelia.<ref>PMID:7600981</ref> <ref>PMID:8939601</ref> <ref>PMID:9076682</ref> <ref>PMID:10427095</ref> <ref>PMID:10688669</ref> <ref>PMID:10811222</ref> <ref>PMID:11493574</ref> <ref>PMID:12421719</ref> <ref>PMID:11941372</ref> <ref>PMID:12574121</ref> <ref>PMID:15548584</ref> <ref>PMID:15936275</ref> <ref>PMID:16026968</ref> <ref>PMID:15677333</ref> <ref>PMID:16362052</ref> <ref>PMID:18552847</ref> <ref>PMID:11970895</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/3fy5_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fy5 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Xenopus laevis]] | ||
| + | [[Category: Earnest T]] | ||
| + | [[Category: Friedland N]] | ||
| + | [[Category: Hung L-W]] | ||
| + | [[Category: Moon R]] | ||
Current revision
Dishevelled PDZ domain homodimer
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