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| | ==Solution structure of the second PDZ domain of Par-3== | | ==Solution structure of the second PDZ domain of Par-3== |
| - | <StructureSection load='2ogp' size='340' side='right'caption='[[2ogp]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2ogp' size='340' side='right'caption='[[2ogp]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ogp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OGP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ogp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OGP FirstGlance]. <br> |
| - | </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=2ogp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ogp OCA], [https://pdbe.org/2ogp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ogp RCSB], [https://www.ebi.ac.uk/pdbsum/2ogp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ogp ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2ogp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ogp OCA], [https://pdbe.org/2ogp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ogp RCSB], [https://www.ebi.ac.uk/pdbsum/2ogp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ogp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PARD3_RAT PARD3_RAT]] Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (By similarity). Targets the phosphatase PTEN to cell junctions.<ref>PMID:18082612</ref> <ref>PMID:18550519</ref>
| + | [https://www.uniprot.org/uniprot/PARD3_RAT PARD3_RAT] Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (By similarity). Targets the phosphatase PTEN to cell junctions.<ref>PMID:18082612</ref> <ref>PMID:18550519</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chan, L N]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Chen, J]] | + | [[Category: Chan L-N]] |
| - | [[Category: Feng, W]] | + | [[Category: Chen J]] |
| - | [[Category: Wu, H]] | + | [[Category: Feng W]] |
| - | [[Category: Zhang, M]] | + | [[Category: Wu H]] |
| - | [[Category: Cell polarity]]
| + | [[Category: Zhang M]] |
| - | [[Category: Par-3]]
| + | |
| - | [[Category: Pdz domain]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
PARD3_RAT Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons (By similarity). Targets the phosphatase PTEN to cell junctions.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Multiple PDZ domain scaffold protein Par-3 and phosphoinositides (PIPs) are required for polarity in diverse cell types. We show that the second PDZ domain of Par-3 binds to phosphatidylinositol (PI) lipid membranes with high affinity. We further demonstrate that a large subset of PDZ domains in mammalian genomes are capable of binding to PI lipid membranes, indicating that lipid binding is the second most prevalent interaction mode of PDZ domains known to date. The biochemical and structural basis of Par-3 PDZ2-mediated membrane interaction is characterized in detail. The membrane binding capacity of Par-3 PDZ2 is critical for epithelial cell polarization. Interestingly, the lipid phosphatase PTEN directly binds to the third PDZ domain of Par-3. The concatenation of the PIP-binding PDZ2 and the lipid phosphatase PTEN-binding PDZ3 endows Par-3 as an ideal scaffold protein for integrating PIP signaling events during cellular polarization.
PDZ domains of Par-3 as potential phosphoinositide signaling integrators.,Wu H, Feng W, Chen J, Chan LN, Huang S, Zhang M Mol Cell. 2007 Dec 14;28(5):886-98. PMID:18082612[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wu H, Feng W, Chen J, Chan LN, Huang S, Zhang M. PDZ domains of Par-3 as potential phosphoinositide signaling integrators. Mol Cell. 2007 Dec 14;28(5):886-98. PMID:18082612 doi:10.1016/j.molcel.2007.10.028
- ↑ Feng W, Wu H, Chan LN, Zhang M. Par-3-mediated junctional localization of the lipid phosphatase PTEN is required for cell polarity establishment. J Biol Chem. 2008 Aug 22;283(34):23440-9. doi: 10.1074/jbc.M802482200. Epub 2008 , Jun 10. PMID:18550519 doi:10.1074/jbc.M802482200
- ↑ Wu H, Feng W, Chen J, Chan LN, Huang S, Zhang M. PDZ domains of Par-3 as potential phosphoinositide signaling integrators. Mol Cell. 2007 Dec 14;28(5):886-98. PMID:18082612 doi:10.1016/j.molcel.2007.10.028
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