Crystallization and preliminary X-ray diffraction studies on the human Plk1 Polo-box domain in complex with an unphosphorylated and a phosphorylated target peptide from Cdc25C.

ABSTRACT: Polo-like kinase (Plk1) is crucial for cell-cycle progression via mitosis. Members of the Polo-like kinase family are characterized by the presence of a C-terminal domain termed the Polo-box domain (PBD) in addition to the N-terminal kinase domain. The PBD of Plk1 was cloned and overexpressed in Escherichia coli. Crystallization experiments of the protein in complex with an unphosphorylated and a phosphorylated target peptide from Cdc25C yield crystals suitable for X-ray diffraction analysis. Crystals of the PBD in complex with the phosphorylated peptide belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 38.23, b = 67.35, c = 88.25 angstroms, alpha = gamma = beta = 90 degrees, and contain one molecule per asymmetric unit. Crystals of the PBD in complex with

SUBMITTER: Garcia-Alvarez B 

PROVIDER: S-EPMC2222578 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature