2ns5
From Proteopedia
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| - | [[Image:2ns5.jpg|left|200px]] | + | [[Image:2ns5.jpg|left|200px]] |
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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''' | + | {{Structure |
| + | |PDB= 2ns5 |SIZE=350|CAPTION= <scene name='initialview01'>2ns5</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= Pard3, Par3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | }} | ||
| + | |||
| + | '''The conserved N-terminal domain of Par-3 adopts a novel PB1-like structure required for Par-3 oligomerization and apical membrane localization''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2NS5 is a [ | + | 2NS5 is a [[Single protein]] structure of 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=2NS5 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17476308 17476308] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signaling protein]] | [[Category: signaling protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:50:24 2008'' |
Revision as of 15:50, 20 March 2008
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| Gene: | Pard3, Par3 (Rattus norvegicus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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