3zee: Difference between revisions
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==Electron cyro-microscopy helical reconstruction of Par-3 N terminal domain== | |||
<StructureSection load='3zee' size='340' side='right' caption='[[3zee]], [[Resolution|resolution]] 6.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zee]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZEE FirstGlance]. <br> | |||
</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=3zee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zee OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zee RCSB], [http://www.ebi.ac.uk/pdbsum/3zee PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Chen, J | [[Category: Chen, J]] | ||
[[Category: Feng, W | [[Category: Feng, W]] | ||
[[Category: Gao, F | [[Category: Gao, F]] | ||
[[Category: Gong, W | [[Category: Gong, W]] | ||
[[Category: Sun, F | [[Category: Sun, F]] | ||
[[Category: Wang, W | [[Category: Wang, W]] | ||
[[Category: Zhang, K | [[Category: Zhang, K]] | ||
[[Category: Zhang, M | [[Category: Zhang, M]] | ||
[[Category: Zhang, Y | [[Category: Zhang, Y]] | ||
[[Category: Cell cycle]] | [[Category: Cell cycle]] | ||
Revision as of 08:53, 21 December 2014
Electron cyro-microscopy helical reconstruction of Par-3 N terminal domain
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