| First Author | Penkert RR | Year | 2004 |
| Journal | Nat Struct Mol Biol | Volume | 11 |
| Issue | 11 | Pages | 1122-7 |
| PubMed ID | 15475968 | Mgi Jnum | J:243405 |
| Mgi Id | MGI:5908345 | Doi | 10.1038/nsmb839 |
| Citation | Penkert RR, et al. (2004) Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex. Nat Struct Mol Biol 11(11):1122-7 |
| abstractText | 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. |
