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2ns5

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Current revision

The conserved N-terminal domain of Par-3 adopts a novel PB1-like structure required for Par-3 oligomerization and apical membrane localization

Structural highlights

2ns5 is a 1 chain structure with sequence from Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

The evolutionarily conserved Par-3/Par-6/aPKC complex is essential for the establishment and maintenance of polarity of a wide range of cells. Both Par-3 and Par-6 are PDZ domain containing scaffold proteins capable of binding to polarity regulatory proteins. In addition to three PDZ domains, Par-3 also contains a conserved N-terminal oligomerization domain (NTD) that is essential for proper subapical membrane localization and consequently the functions of Par-3. The molecular basis of NTD-mediated Par-3 membrane localization is poorly understood. Here, we describe the structure of a monomeric form of the Par-3 NTD. Unexpectedly, the domain adopts a PB1-like fold with both type-I and type-II structural features. The Par-3 NTD oligomerizes into helical filaments via front-to-back interactions. We further demonstrate that the NTD-mediated membrane localization of Par-3 in MDCK cells is solely attributed to its oligomerization capacity. The data presented in this study suggest that the Par-3 NTD is likely to facilitate the assembly of higher-order Par-3/Par-6/aPKC complex with increased avidities in targeting the complex to the subapical membrane domain and in binding to other polarity-regulating proteins.

The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization.,Feng W, Wu H, Chan LN, Zhang M EMBO J. 2007 Jun 6;26(11):2786-96. Epub 2007 May 3. PMID:17476308^[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
↑ Feng W, Wu H, Chan LN, Zhang M. The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization. EMBO J. 2007 Jun 6;26(11):2786-96. Epub 2007 May 3. PMID:17476308

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ns5"

@@ Line 1: / Line 1: @@
 ==The conserved N-terminal domain of Par-3 adopts a novel PB1-like structure required for Par-3 oligomerization and apical membrane localization==
-<StructureSection load='2ns5' size='340' side='right'caption='[[2ns5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2ns5' size='340' side='right'caption='[[2ns5]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ns5]] 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=2NS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NS5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ns5]] 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=2NS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NS5 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pard3, Par3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=2ns5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ns5 OCA], [https://pdbe.org/2ns5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ns5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ns5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ns5 ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
 [[Category: Large Structures]]
-[[Category: Chan, L N]]
+[[Category: Rattus norvegicus]]
-[[Category: Feng, W]]
+[[Category: Chan L-N]]
-[[Category: Wu, H]]
+[[Category: Feng W]]
-[[Category: Zhang, M]]
+[[Category: Wu H]]
-[[Category: Asymmetric membrane localization]]
+[[Category: Zhang M]]
-[[Category: Cell polarity]]
-[[Category: N-terminal domain]]
-[[Category: Par-3]]
-[[Category: Pb1 domain]]
-[[Category: Signaling protein]]

2ns5

From Proteopedia

Current revision

The conserved N-terminal domain of Par-3 adopts a novel PB1-like structure required for Par-3 oligomerization and apical membrane localization

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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