Ravichandran N. Murugan" /> " /> Song Yub Shin " /> Chaejoon Cheong" /> Kyung S Lee " /> Ravichandran N. Murugan, Jung-Eun Park, Eun-Hee Kim, Song Yub Shin, Chaejoon Cheong, Kyung S Lee, and Jeong Kyu Bang*

" /> Ravichandran N. Murugan, Jung-Eun Park, Eun-Hee Kim, Song Yub Shin, Chaejoon Cheong, Kyung S Lee, and Jeong Kyu Bang*

. Mol. Cells 2011;32:209-20. https://doi.org/10.1007/s10059-011-0126-3">
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Mol. Cells 2011; 32(3): 209-220

Published online September 30, 2011

https://doi.org/10.1007/s10059-011-0126-3

© The Korean Society for Molecular and Cellular Biology

Plk1-Targeted Small Molecule Inhibitors: Molecular Basis for Their Potency and Specificity

Ravichandran N. Murugan, Jung-Eun Park1, Eun-Hee Kim, Song Yub Shin2, Chaejoon Cheong, Kyung S Lee1, and Jeong Kyu Bang*

Division of Magnetic Resonance, Korea Basic Science Institute, Ochang 363-883, Korea, 1Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA, 2Department of Cellular & Molecular Medicine, School of Medicine, Chosun University, Gwangju 501-759, Korea

Correspondence to : *Correspondence: bangjk@kbsi.re.kr

Received: June 17, 2011; Accepted: June 23, 2011

Abstract

Members of polo-like kinases (collectively, Plks) have been identified in various eukaryotic organisms and play pivotal roles in cell proliferation. They are characterized by the presence of a distinct region of homology in the C-terminal noncatalytic domain, called polo-box domain (PBD). Among them, Plk1 and its functional homologs in other organisms have been best characterized because of its strong association with tumorigenesis. Plk1 is overexpressed in a wide spectrum of cancers in humans, and is thought to be an attractive anti-cancer drug target. Plk1 offers, within one molecule, two functionally different drug targets with distinct properties-the N-terminal catalytic domain and the C-terminal PBD essential for targeting the catalytic activity of Plk1 to specific subcellular locations. In this review, we focused on discussing the recent development of small-molecule and phosphopeptide inhibitors for their potency and specificity against Plk1. Our effort in understanding the binding mode of various inhibitors to Plk1 PBD are also presented.

Keywords cancer therapy, inhibitors, Plk1, polo-box domain (PBD), polo-like kinase

Article

Minireview

Mol. Cells 2011; 32(3): 209-220

Published online September 30, 2011 https://doi.org/10.1007/s10059-011-0126-3

Copyright © The Korean Society for Molecular and Cellular Biology.

Plk1-Targeted Small Molecule Inhibitors: Molecular Basis for Their Potency and Specificity

Ravichandran N. Murugan, Jung-Eun Park1, Eun-Hee Kim, Song Yub Shin2, Chaejoon Cheong, Kyung S Lee1, and Jeong Kyu Bang*

Division of Magnetic Resonance, Korea Basic Science Institute, Ochang 363-883, Korea, 1Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA, 2Department of Cellular & Molecular Medicine, School of Medicine, Chosun University, Gwangju 501-759, Korea

Correspondence to:*Correspondence: bangjk@kbsi.re.kr

Received: June 17, 2011; Accepted: June 23, 2011

Abstract

Members of polo-like kinases (collectively, Plks) have been identified in various eukaryotic organisms and play pivotal roles in cell proliferation. They are characterized by the presence of a distinct region of homology in the C-terminal noncatalytic domain, called polo-box domain (PBD). Among them, Plk1 and its functional homologs in other organisms have been best characterized because of its strong association with tumorigenesis. Plk1 is overexpressed in a wide spectrum of cancers in humans, and is thought to be an attractive anti-cancer drug target. Plk1 offers, within one molecule, two functionally different drug targets with distinct properties-the N-terminal catalytic domain and the C-terminal PBD essential for targeting the catalytic activity of Plk1 to specific subcellular locations. In this review, we focused on discussing the recent development of small-molecule and phosphopeptide inhibitors for their potency and specificity against Plk1. Our effort in understanding the binding mode of various inhibitors to Plk1 PBD are also presented.

Keywords: cancer therapy, inhibitors, Plk1, polo-box domain (PBD), polo-like kinase

Mol. Cells
Nov 30, 2022 Vol.45 No.11, pp. 763~867
COVER PICTURE
Naive (cyan) and axotomized (magenta) retinal ganglion cell axons in Xenopus tropicalis (Choi et al., pp. 846-854).

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