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Structural and Functional Analyses of Minimal Phosphopeptides Targeting the Polo-Box Domain of Polo-Like Kinase 1

Structural and Functional Analyses of Minimal Phosphopeptides Targeting the Polo-Box Domain of Polo-Like Kinase 1

Sang-Moon Yun, Tinoush Moulaei, Dan Lim, Jeong K Bang, Jung-Eun Park, Shilpa R Shenoy, Fa Liu, Young H Kang, Chenzhong Liao, Nak-Kyun Soung, Sunhee Lee, Do-Young Yoon, Yoongho Lim, Dong-Hee Lee, Akira Otaka, etc.

Nat Struct Mol Biol. 2009 Aug;16(8):876-82.

PMID: 19597481

Abstract:

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 complex with the minimal phosphopeptides revealed that the C-terminal SpT dipeptide functions as a high-affinity anchor, whereas the N-terminal residues are crucial for providing specificity and affinity to the interaction. Inhibition of the PLK1 PBD by phosphothreonine mimetic peptides was sufficient to induce mitotic arrest and apoptotic cell death. The mode of interaction between the minimal peptide and PBD may provide a template for designing therapeutic agents that target PLK1.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42416153	PLK3 Polo Box Domain human			Price

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