5oak: Difference between revisions

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-'''Unreleased structure'''
-The entry 5oak is ON HOLD  until Paper Publication
+==Structure of the dmPar3 PDZ1 domain in complex with the dmPar6 PBM==
+<StructureSection load='5oak' size='340' side='right'caption='[[5oak]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5oak]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OAK 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]] 1.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5oak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oak OCA], [https://pdbe.org/5oak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oak RCSB], [https://www.ebi.ac.uk/pdbsum/5oak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oak ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/X2JFU8_DROME X2JFU8_DROME]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Polarity is a fundamental property of most cell types. The Par protein complex is a major driving force in generating asymmetrically localized protein networks and consists of atypical protein kinase C (aPKC), Par3, and Par6. Dysfunction of this complex causes developmental abnormalities and diseases such as cancer. We identified a PDZ domain-binding motif in Par6 that was essential for its interaction with Par3 in vitro and for Par3-mediated membrane localization of Par6 in cultured cells. In fly embryos, we observed that the PDZ domain-binding motif was functionally redundant with the PDZ domain in targeting Par6 to the cortex of epithelial cells. Our structural analyses by x-ray crystallography and NMR spectroscopy showed that both the PDZ1 and PDZ3 domains but not the PDZ2 domain in Par3 engaged in a canonical interaction with the PDZ domain-binding motif in Par6. Par3 thus has the potential to recruit two Par6 proteins simultaneously, which may facilitate the assembly of polarity protein networks through multivalent PDZ domain interactions.
-Authors:
+Structural basis for the interaction between the cell polarity proteins Par3 and Par6.,Renschler FA, Bruekner SR, Salomon PL, Mukherjee A, Kullmann L, Schutz-Stoffregen MC, Henzler C, Pawson T, Krahn MP, Wiesner S Sci Signal. 2018 Feb 13;11(517). pii: 11/517/eaam9899. doi:, 10.1126/scisignal.aam9899. PMID:29440511<ref>PMID:29440511</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5oak" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Drosophila melanogaster]]
+[[Category: Large Structures]]
+[[Category: Bruekner SR]]
+[[Category: Wiesner S]]