4J7B

Crystal structure of polo-like kinase 1

Summary for 4J7B

• Entry DOI: 10.2210/pdb4j7b/pdb
• Descriptor: Polo-like kinase, 205 kDa microtubule-associated protein, ... (4 entities in total)
• Functional Keywords: first complex structure of kd and pbd domain, regulator of mitosis, phosphorylated target protein, transferase
• Biological source: Danio rerio (leopard danio,zebra danio,zebra fish); More
• Cellular location: Cytoplasm, cytoskeleton: P23226
• Total number of polymer chains: 6
• Total formula weight: 135998.81

Authors

Xu, J.,Shen, C.,Quan, J.,Wang, T. (deposition date: 2013-02-13, release date: 2013-07-24, Last modification date: 2023-11-08)

Primary citation

Xu, J.,Shen, C.,Wang, T.,Quan, J.
Structural basis for the inhibition of Polo-like kinase 1
Nat.Struct.Mol.Biol., 20:1047-1053, 2013

PubMed Abstract: 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-Å 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.

PubMed: 23893132
DOI: 10.1038/nsmb.2623

Experimental method

X-RAY DIFFRACTION (2.3 Å)