Crystal structure of a wildtype Polo-like kinase 1 (Plk1) catalytic domain.

Structures of the wild-type and activated catalytic domains of Brachydanio rerio Polo-like kinase 1 (Plk1): changes in the active-site conformation and interactions with ligands.

Side-scattering cube root I-beam bent single crystal; asymmetric cut 12.2 degs. Crystal type: Si(311)

GPLGSMSAAIAKPSAKPSAHVDPKSAPLKEIPDVLVDPRTMKRYMRGRFLGKGGFAKCYEITDMDTKEVFAGKVVPKSML
LKPHQKEKMSTEIAIHKSLDNPHVVGFHGFFEDDDFVYVVLEICRRRSLLELHKRRKAVTEPEARYFMRQTIQGVQYLHN
NRVIHRDLKLGNLFLNDDMDVKIGDFGLATKIEFDGERKKTLCGTPNYIAPEVLCKKGHSFEVDIWSLGCILYTLLVGKP
PFETSCLKETYIRIKKNEYSVPRHINPVASALIRRMLHADPTLRPSVAELLTDEFFTSGYAPMRLPTSCLTVPPRFS

hanging-drop vapor diffusion at 4 C (277K); protein at 7 mg/ml in 50 mM Tris-HCl pH 7.5, 200 mM NaCl and 3 mM DTT; crystallization condition: 0.1 M tri-sodium citrate pH 5.6, 0.2 M (NH4)2SO4, and 25% PEG 3350; cryoprotectant: paraffin oil., VAPOR DIFFUSION, HANGING DROP

Polo-like kinase 1, Plk1, catalytic domain, small-molecule inhibitor, Kinase, TRANSFERASE

MSAAIAKPSAKPSAHVDPKSAPLKEIPDVLVDPRTMKRYMRGRFLGKGGFAKCYEITDMDTKEVFAGKVVPKSMLLKPHQ
KEKMSTEIAIHKSLDNPHVVGFHGFFEDDDFVYVVLEICRRRSLLELHKRRKAVTEPEARYFMRQTIQGVQYLHNNRVIH
RDLKLGNLFLNDDMDVKIGDFGLATKIEFDGERKKTLCGTPNYIAPEVLCKKGHSFEVDIWSLGCILYTLLVGKPPFETS
CLKETYIRIKKNEYSVPRHINPVASALIRRMLHADPTLRPSVAELLTDEFFTSGYAPMRLPTSCLTVPPRFS