2NS5

The conserved N-terminal domain of Par-3 adopts a novel PB1-like structure required for Par-3 oligomerization and apical membrane localization

Summary for 2NS5

• Entry DOI: 10.2210/pdb2ns5/pdb
• Descriptor: Partitioning-defective 3 homolog (1 entity in total)
• Functional Keywords: cell polarity, par-3, n-terminal domain, pb1 domain, asymmetric membrane localization, signaling protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Endomembrane system: Q9Z340
• Total number of polymer chains: 1
• Total formula weight: 9683.95

Authors

Feng, W.,Wu, H.,Chan, L.-N.,Zhang, M. (deposition date: 2006-11-03, release date: 2007-09-04, Last modification date: 2023-12-27)

Primary citation

Feng, W.,Wu, H.,Chan, L.-N.,Zhang, M.
The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization
Embo J., 26:2786-2796, 2007

PubMed Abstract: 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.

PubMed: 17476308
DOI: 10.1038/sj.emboj.7601702

Experimental method

SOLUTION NMR