Exploring the binding nature of pyrrolidine pocket-dependent interactions in the polo-box domain of polo-like kinase 1
Murugan, R.N., Ahn, M., Lee, W.C., Kim, H.Y., Song, J.H., Cheong, C., Hwang, E., Seo, J.H., Shin, S.Y., Choi, S.H., Park, J.E., Bang, J.K.(2013) PLoS One 8: e80043-e80043
- PubMed: 24223211 
- DOI: https://doi.org/10.1371/journal.pone.0080043
- Primary Citation of Related Structures:  
4LKL, 4LKM - PubMed Abstract: 
Over the years, a great deal of effort has been focused on the design and synthesis of potent, linear peptide inhibitors targeting the polo-like kinase 1 (Plk1), which is critically involved in multiple mitotic processes and has been established as an adverse prognostic marker for tumor patients. Plk1 localizes to its intracellular anchoring sites via its polo-box domain, and inhibiting the Plk1 polo-box domain has been considered as an approach to circumvent the specificity problems associated with inhibiting the conserved adenosine triphosphate-binding pocket. The polo-box domain consists of two different binding regions, such as the unique, broader pyrrolidine-binding pocket and the conserved, narrow, Tyr-rich hydrophobic channel, among the three Plk polo-box domains (Plks 1-3), respectively. Therefore, the studies that provide insights into the binding nature of the unique, broader pyrrolidine-binding pocket might lead to the development of selective Plk1-inhibitory compounds.
Organizational Affiliation: 
Division of Magnetic Resonance, Korea Basic Science Institute, Ochang, Chung-Buk, Republic of Korea.