1X8S

Structure of the Par-6 PDZ domain with a Pals1 internal ligand

Summary for 1X8S

• Entry DOI: 10.2210/pdb1x8s/pdb
• Descriptor: CG5884-PA, Pals1 peptide (3 entities in total)
• Functional Keywords: cell cycle, par-6
• Biological source: Drosophila melanogaster (fruit fly); More
• Total number of polymer chains: 2
• Total formula weight: 12375.15

Authors

Penkert, R.R.,DiVittorio, H.M.,Prehoda, K.E. (deposition date: 2004-08-18, release date: 2004-12-07, Last modification date: 2024-02-14)

Primary citation

Penkert, R.R.,Divittorio, H.M.,Prehoda, K.E.
Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex.
Nat.Struct.Mol.Biol., 11:1122-1127, 2004

PubMed Abstract: PDZ protein interaction domains are typically selective for C-terminal ligands, but non-C-terminal, 'internal' ligands have also been identified. The PDZ domain from the cell polarity protein Par-6 binds C-terminal ligands and an internal sequence from the protein Pals1/Stardust. The structure of the Pals1-Par-6 PDZ complex reveals that the PDZ ligand-binding site is deformed to allow for internal binding. Whereas binding of the Rho GTPase Cdc42 to a CRIB domain adjacent to the Par-6 PDZ regulates binding of C-terminal ligands, the conformational change that occurs upon binding of Pals1 renders its binding independent of Cdc42. These results suggest a mechanism by which the requirement for a C terminus can be readily bypassed by PDZ ligands and reveal a complex set of cooperative and competitive interactions in Par-6 that are likely to be important for cell polarity regulation.

PubMed: 15475968
DOI: 10.1038/nsmb839

Experimental method

X-RAY DIFFRACTION (2.503 Å)