1x8s
Structure of the Par-6 PDZ domain with a Pals1 internal ligandStructure of the Par-6 PDZ domain with a Pals1 internal ligand
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPDZ 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. Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex.,Penkert RR, DiVittorio HM, Prehoda KE Nat Struct Mol Biol. 2004 Nov;11(11):1122-7. Epub 2004 Oct 10. PMID:15475968[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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