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| | ==Crystal structure of Par3-NTD domain== | | ==Crystal structure of Par3-NTD domain== |
| - | <StructureSection load='4i6p' size='340' side='right' caption='[[4i6p]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='4i6p' size='340' side='right'caption='[[4i6p]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4i6p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I6P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4i6p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I6P FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zee|3zee]]</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]] 2.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pard3, Par3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=4i6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i6p OCA], [https://pdbe.org/4i6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i6p RCSB], [https://www.ebi.ac.uk/pdbsum/4i6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i6p ProSAT]</span></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=4i6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i6p OCA], [http://pdbe.org/4i6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i6p RCSB], [http://www.ebi.ac.uk/pdbsum/4i6p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i6p ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Feng, W]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Gao, F]] | + | [[Category: Feng W]] |
| - | [[Category: Gong, W]] | + | [[Category: Gao F]] |
| - | [[Category: Sun, F]] | + | [[Category: Gong W]] |
| - | [[Category: Wang, W]] | + | [[Category: Sun F]] |
| - | [[Category: Cell polarity protein]]
| + | [[Category: Wang W]] |
| - | [[Category: Duf3534]]
| + | |
| - | [[Category: Pb1 like motif]]
| + | |
| - | [[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]
Publication Abstract from PubMed
Par-3, the central organizer of the Par-3/Par-6/atypical protein kinase C complex, is a multimodular scaffold protein that is essential for cell polarity establishment and maintenance. The N-terminal domain (NTD) of Par-3 is capable of self-association to form filament-like structures, although the underlying mechanism is poorly understood. Here, we determined the crystal structure of Par-3 NTD and solved the filament structure by cryoelectron microscopy. We found that an intrinsic "front-to-back" interaction mode is important for Par-3 NTD self-association and that both the lateral and longitudinal packing within the filament are mediated by electrostatic interactions. Disruptions of the lateral or longitudinal packing significantly impaired Par-3 NTD self-association and thereby impacted the Par-3-mediated epithelial polarization. We finally demonstrated that a Par-3 NTD-like domain from histidine ammonia-lyase also harbors a similar self-association capacity. This work unequivocally provides the structural basis for Par-3 NTD self-association and characterizes one type of protein domain that can self-assemble via electrostatic interactions.
Structural insights into the intrinsic self-assembly of par-3 N-terminal domain.,Zhang Y, Wang W, Chen J, Zhang K, Gao F, Gao B, Zhang S, Dong M, Besenbacher F, Gong W, Zhang M, Sun F, Feng W Structure. 2013 Jun 4;21(6):997-1006. doi: 10.1016/j.str.2013.04.004. Epub 2013, May 2. PMID:23643951[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
- ↑ Zhang Y, Wang W, Chen J, Zhang K, Gao F, Gao B, Zhang S, Dong M, Besenbacher F, Gong W, Zhang M, Sun F, Feng W. Structural insights into the intrinsic self-assembly of par-3 N-terminal domain. Structure. 2013 Jun 4;21(6):997-1006. doi: 10.1016/j.str.2013.04.004. Epub 2013, May 2. PMID:23643951 doi:10.1016/j.str.2013.04.004
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