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Literature summary for 2.7.11.21 extracted from

  • Shan, H.M.; Wang, T.; Quan, J.M.
    Crystal structure of the polo-box domain of polo-like kinase 2 (2015), Biochem. Biophys. Res. Commun., 456, 780-784.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant GST-tagged PLK2 (residues 451-685) proteins in Escherichia coli strain BL21 (DE3) pLysS Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
polo-box domain of polo-like kinase 2, residues 451-685, hanging drop vapour diffusion method, mixing of 9 mg/ml protein in 20 mM Tris, 500 mM NaCl, 1 mM DTT, pH 8.0, with crystallization solution containing 35% v/v Tacsimate TM, pH 7.0, 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using the crystal structure of PBD1, PDB ID 1UMW, encompassing residues 373-595 as template Homo sapiens

Protein Variants

Protein Variants Comment Organism
H629A site-directed mutagenesis, the mutation eliminates the capability of PBD2 binding with the phosphopeptide Homo sapiens
K631M site-directed mutagenesis, the mutation eliminates the capability of PBD2 binding with the phosphopeptide Homo sapiens
W507F site-directed mutagenesis, the mutation eliminates the capability of PBD2 binding with the phosphopeptide Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26000
-
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9NYY3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant GST-tagged PLK2 (residues 451-685) proteins from Escherichia coli strain BL21 (DE3) pLysS by glutathione affinity chromatography, followed by tag cleavage by 3C precision protease, another step of glutathione affinity chromatography, and gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information polo-box domain of polo-like kinase 2, residues 451-685, PBD2 binds phosphopeptides containing a SerpSer/pThr motif Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
? x * 26000, about, recombinant polo-box domain of polo-like kinase 2, residues 451-685, SDS-PAGE Homo sapiens
More enzyme PLK2 is characterized by the conserved N-terminal kinase domain and the unique C-terminal polo-box domain (PBD). The PBD mediates diverse functions of PLK2 by binding phosphorylated SerpSer/pThr motifs of its substrates Homo sapiens

Synonyms

Synonyms Comment Organism
Plk2
-
Homo sapiens
polo-like kinase 2
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens

General Information

General Information Comment Organism
evolution the enzyme is a member of the polo-like kinase family. Among the five members, PLK2 is the more closely related to PLK1. The overall structure of the PLK2 PBD is similar to that of the PLK1 PBD, which is composed by two polo boxes each contain b6a structures that form a 12-stranded b sandwich domain. The edge of the interface between the two polo boxes forms the phosphorylated Ser-pSer/pThr motifs binding cleft. On the hand, the peripheral regions around the core binding cleft of the PLK2 PBD is distinct from that of the PLK1 PBD, which might confer the substrate specificity of the PBDs of the polo-like kinase family. Comparison of PLK1 and PL2 substrate binding and structure, detailed overview Homo sapiens
physiological function polo-like kinase 2 (PLK2) is a crucial regulator in cell cycle progression, DNA damage response, and neuronal activity Homo sapiens