5OAK

Structure of the dmPar3 PDZ1 domain in complex with the dmPar6 PBM

Summary for 5OAK

• Entry DOI: 10.2210/pdb5oak/pdb
• Descriptor: Bazooka, isoform C,LD29223p, GLYCEROL (3 entities in total)
• Functional Keywords: cell polarity protein, protein binding
• Biological source: Drosophila melanogaster (Fruit fly); More
• Total number of polymer chains: 4
• Total formula weight: 49103.21

Authors

Bruekner, S.R.,Wiesner, S. (deposition date: 2017-06-22, release date: 2018-02-21, Last modification date: 2024-01-17)

Primary citation

Renschler, F.A.,Bruekner, S.R.,Salomon, P.L.,Mukherjee, A.,Kullmann, L.,Schutz-Stoffregen, M.C.,Henzler, C.,Pawson, T.,Krahn, M.P.,Wiesner, S.
Structural basis for the interaction between the cell polarity proteins Par3 and Par6.
Sci Signal, 11:-, 2018

PubMed Abstract: Polarity is a fundamental property of most cell types. The Par protein complex is a major driving force in generating asymmetrically localized protein networks and consists of atypical protein kinase C (aPKC), Par3, and Par6. Dysfunction of this complex causes developmental abnormalities and diseases such as cancer. We identified a PDZ domain-binding motif in Par6 that was essential for its interaction with Par3 in vitro and for Par3-mediated membrane localization of Par6 in cultured cells. In fly embryos, we observed that the PDZ domain-binding motif was functionally redundant with the PDZ domain in targeting Par6 to the cortex of epithelial cells. Our structural analyses by x-ray crystallography and NMR spectroscopy showed that both the PDZ1 and PDZ3 domains but not the PDZ2 domain in Par3 engaged in a canonical interaction with the PDZ domain-binding motif in Par6. Par3 thus has the potential to recruit two Par6 proteins simultaneously, which may facilitate the assembly of polarity protein networks through multivalent PDZ domain interactions.

PubMed: 29440511
DOI: 10.1126/scisignal.aam9899

Experimental method

X-RAY DIFFRACTION (1.5 Å)