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[[Image:2ns5.png|left|200px]]


{{STRUCTURE_2ns5| PDB=2ns5 | SCENE= }}
==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]]' scene=''>
== Structural highlights ==
<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='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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ns/2ns5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ns5 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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 conserved N-terminal domain of Par-3 adopts a novel PB1-like structure required for Par-3 oligomerization and apical membrane localization===
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<ref>PMID:17476308</ref>


{{ABSTRACT_PUBMED_17476308}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2ns5" style="background-color:#fffaf0;"></div>
[[2ns5]] is a 1 chain structure with sequence from [http://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].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:017476308</ref><references group="xtra"/>
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Chan, L N.]]
[[Category: Chan L-N]]
[[Category: Feng, W.]]
[[Category: Feng W]]
[[Category: Wu, H.]]
[[Category: Wu H]]
[[Category: Zhang, M.]]
[[Category: Zhang M]]
[[Category: Asymmetric membrane localization]]
[[Category: Cell polarity]]
[[Category: N-terminal domain]]
[[Category: Par-3]]
[[Category: Pb1 domain]]
[[Category: Signaling protein]]
Retrieved from "https://proteopedia.org/2ns5"