4j7b | pdb_00004j7b

Crystal structure of polo-like kinase 1

spinqualitylabelsall models 4j7b, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4j7b is a 6 chain structure with sequence from Brachidanio rerio and Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: plk1 (Brachidanio rerio), Map205, CG1483 (DROME) Activity: Polo kinase, with EC number 2.7.11.21 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [MA205_DROME] May play an important role in the regulation of microtubule assembly and interaction. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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