2ns5
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(New page: 200px<br /><applet load="2ns5" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ns5" /> '''The conserved N-terminal domain of Par-3 ado...)
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Revision as of 11:46, 23 January 2008
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The conserved N-terminal domain of Par-3 adopts a novel PB1-like structure required for Par-3 oligomerization and apical membrane localization
Overview
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.
About this Structure
2NS5 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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
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