View source for 4i6p


==Crystal structure of Par3-NTD domain==
<StructureSection load='4i6p' size='340' side='right'caption='[[4i6p]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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>
</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> 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:23643951</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4i6p" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Feng W]]
[[Category: Gao F]]
[[Category: Gong W]]
[[Category: Sun F]]
[[Category: Wang W]]