Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1

@inproceedings{Yun2009StructuralAF,
  title={Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1},
  author={Sang-Moon Yun and Tinoush Moulaei and Dan Lim and Jeong Kyu Bang and Jung-Eun Park and Shilpa R. Shenoy and Fa Liu and Young Hwi Kang and Chenzhong Liao and Nak-Kyun Soung and Sunhee Lee and Do-Young Yoon and Yoongho Lim and Dong-Hee Lee and Akira Otaka and Ettore Appella and James B. Mcmahon and Marc C. Nicklaus and Terrence R. Burke and Michael B. Yaffe and Alexander Wlodawer and Kyung S Lee},
  booktitle={Nature Structural &Molecular Biology},
  year={2009}
}
Polo-like kinase-1 (Plk1) has a pivotal role in cell proliferation and is considered a potential target for anticancer therapy. The noncatalytic polo-box domain (PBD) of Plk1 forms a phosphoepitope binding module for protein-protein interaction. Here, we report the identification of minimal phosphopeptides that specifically interact with the PBD of human PLK1, but not those of the closely related PLK2 and PLK3. Comparative binding studies and analyses of crystal structures of the PLK1 PBD in… CONTINUE READING
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