5oak: Difference between revisions
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==Structure of the dmPar3 PDZ1 domain in complex with the dmPar6 PBM== | |||
<StructureSection load='5oak' size='340' side='right'caption='[[5oak]], [[Resolution|resolution]] 1.50Å' 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]] 1.5Å</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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </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]] | |||
Latest revision as of 12:38, 6 December 2023
Structure of the dmPar3 PDZ1 domain in complex with the dmPar6 PBMStructure of the dmPar3 PDZ1 domain in complex with the dmPar6 PBM
Structural highlights
FunctionPublication Abstract from PubMedPolarity 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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