Structural highlights
Function
Q6DRK7_DANRE
Publication Abstract from PubMed
Polo-like kinase 1 (PLK1) is a master regulator of mitosis and is considered a potential drug target for cancer therapy. PLK1 is characterized by an N-terminal kinase domain (KD) and a C-terminal Polo-box domain (PBD). The KD and PBD are mutually inhibited, but the molecular mechanisms of the autoinhibition remain unclear. Here we report the 2.3-A crystal structure of the complex of the Danio rerio KD and PBD together with a PBD-binding motif of Drosophila melanogaster microtubule-associated protein 205 (Map205(PBM)). The structure reveals that the PBD binds and rigidifies the hinge region of the KD in a distinct conformation from that of the phosphopeptide-bound PBD. This structure provides a framework for understanding the autoinhibitory mechanisms of PLK1 and also sheds light on the activation mechanisms of PLK1 by phosphorylation or phosphopeptide binding.
Structural basis for the inhibition of Polo-like kinase 1.,Xu J, Shen C, Wang T, Quan J Nat Struct Mol Biol. 2013 Sep;20(9):1047-53. doi: 10.1038/nsmb.2623. Epub 2013, Jul 28. PMID:23893132[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu J, Shen C, Wang T, Quan J. Structural basis for the inhibition of Polo-like kinase 1. Nat Struct Mol Biol. 2013 Sep;20(9):1047-53. doi: 10.1038/nsmb.2623. Epub 2013, Jul 28. PMID:23893132 doi:10.1038/nsmb.2623
