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The polo-box domain (PBD) present in Plk1's C-terminal non-catalytic region has been shown to play a central role in targeting the N-terminal kinase domain of Plk1 to specific subcellular locations. Subsequent studies reveal that PBD binds to a phosphorylated motif generated by one of the two mechanisms - self-priming by Plk1 itself or non.
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The POLO-Box domain is exclusively found in the family of Polo-like kinases that regulate mitotic entry, spindle assembly, centrosome maturation, chromosome segregation, cytokinesis and cell cycle arrest. The approximately 200 amino acid POLO-Box domain consists of two highly conserved Polo Box motifs of ~70-80 amino acids each, and is.
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Introduction. Polo-like kinase 1 (PLK1), a member of the Polo-like kinase (PLK) family, is an enzyme mainly involved in cell cycle progression , .PLKs consist of an N-terminal Ser/Thr kinase domain and a C-terminal regulatory Polo-box domain (PBD), which is characteristic for this family of kinases .The PBD is crucial for the ligand binding and subcellular localization of kinases .
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Polo-like kinase 1 (PLK1) is a key regulator enzyme of cell cycle progression, which belongs to a kinase family named Polo-like kinases [1, 2].This family is characterized by a C-terminal domain termed Polo-box domain (PBD), which represents a regulatory domain for the function of the N-terminal Ser/Thr kinase domain [].PLK1 is activated during mitosis [].
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The polo-box domain: a molecular integrator of mitotic kinase cascades and polo-like kinase function. Cell Cycle. 2004; 3:128-31. doi: 10.4161/cc.3.2.660. [Google Scholar] Luo J, Emanuele MJ, Li D, Creighton CJ, Schlabach MR, Westbrook TF, Wong KK, Elledge SJ. A genome-wide RNAi screen identifies multiple synthetic lethal interactions with.
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Polo-like kinases (Plks) are the key regulators of cell cycle progression, the members of which share a kinase domain and a polo-box domain (PBD) that serves as a protein-binding module. While Plk1 is a promising target for antitumor therapy, Plk2 is regarded as a tumor suppressor even though the two Plks commonly recognize the S-pS/T-P motif.
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If this was the case, Glu86 would bind close to Asp611 and Asp631 from polo-box domain, and this could explain why a Dbf4-E86K peptide binds to the polo-box domain of Cdc5 with higher affinity.
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