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3FVH

Polo-like kinase 1 Polo box domain in complex with Ac-LHSpTA-NH2 peptide

Summary for 3FVH
Entry DOI10.2210/pdb3fvh/pdb
DescriptorSerine/threonine-protein kinase PLK1, Acetyl-Leu-His-Ser-phosphoThr-Ala-NH2 peptide (3 entities in total)
Functional Keywordspolo like kinase 1, polo box domain, phosphopeptide binding domain, atp-binding, cell cycle, cell division, kinase, mitosis, nucleotide-binding, nucleus, phosphoprotein, serine/threonine-protein kinase, transferase, peptide binding protein
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus: P53350
Total number of polymer chains2
Total formula weight27917.76
Authors
Lim, D.C.,Yaffe, M.B. (deposition date: 2009-01-15, release date: 2009-08-04, Last modification date: 2024-11-27)
Primary citationYun, S.M.,Moulaei, T.,Lim, D.,Bang, J.K.,Park, J.E.,Shenoy, S.R.,Liu, F.,Kang, Y.H.,Liao, C.,Soung, N.K.,Lee, S.,Yoon, D.Y.,Lim, Y.,Lee, D.H.,Otaka, A.,Appella, E.,McMahon, J.B.,Nicklaus, M.C.,Burke, T.R.,Yaffe, M.B.,Wlodawer, A.,Lee, K.S.
Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1
Nat.Struct.Mol.Biol., 16:876-882, 2009
Cited by
PubMed 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.
PubMed: 19597481
DOI: 10.1038/nsmb.1628
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.58 Å)
Structure validation

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