Structural basis for the inhibition of Polo-like kinase 1

@article{Xu2013StructuralBF,
  title={Structural basis for the inhibition of Polo-like kinase 1},
  author={Jun Xu and Chen Shen and Tian J. Wang and Junmin Quan},
  journal={Nature Structural &Molecular Biology},
  year={2013},
  volume={20},
  pages={1047-1053}
}
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… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 27 extracted citations

Plk1 regulates MEK1/2 and proliferation in airway smooth muscle cells

Respiratory research • 2015
View 4 Excerpts
Highly Influenced

References

Publications referenced by this paper.
Showing 1-10 of 66 references

A mechanism for tunable autoinhibition in the structure of a human Ca 2 + / calmodulin - dependent kinase II holoenzyme

L. H. Chao
Cell • 2011

Overview of the CCP4 suite and current developments

Winn, M.D
Acta Crystallogr. D Biol. Crystallogr • 2011

prediction and discovery of a binding site on the surface of polo-like kinase 1

Śledź, P. et al. From crystal packing to molecular recognition
Angew. Chem. Int. Edn Engl. 50, 4003–4006 • 2011

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Acta crystallographica. Section D, Biological crystallography • 2010

a comprehensive Python-based system for macromolecular structure solution

Adams, P. D. et al. PHENIX
Acta Crystallogr. D Biol. Crystallogr. 66, 213–221 • 2010

Similar Papers

Loading similar papers…