First (cryptic) polo-box domain (PBD) of polo-like kinase 4 (Plk4/Sak)
The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides.
Structure:4G7N: The first cryptic POLO box domain of Drosophila melanogaster Plk4 participates in homodimerization, contacts at 4A - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",