4RS6

Crystal structure of the C domain of Polo like Kinase II in Homo Sapiens

Summary for 4RS6

• Entry DOI: 10.2210/pdb4rs6/pdb
• Descriptor: Serine/threonine-protein kinase PLK2 (2 entities in total)
• Functional Keywords: first pbd domain of polo like kinase ii, phosphorylation of target protein, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole : Q9NYY3
• Total number of polymer chains: 2
• Total formula weight: 54888.18

Authors

Shan, H.,Quan, J.,Wang, T. (deposition date: 2014-11-07, release date: 2014-12-03, Last modification date: 2023-11-08)

Primary citation

Shan, H.M.,Wang, T.,Quan, J.M.
Crystal structure of the polo-box domain of polo-like kinase 2
Biochem.Biophys.Res.Commun., 456:780-784, 2015

PubMed Abstract: Polo-like kinase 2 (PLK2) is a crucial regulator in cell cycle progression, DNA damage response, and neuronal activity. 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 Ser-pSer/pThr motifs of its substrates. Here, we report the first crystal structure of the PBD of PLK2. The overall structure of the PLK2 PBD is similar to that of the PLK1 PBD, which is composed by two polo boxes each contain β6α structures that form a 12-stranded β 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.

PubMed: 25511705
DOI: 10.1016/j.bbrc.2014.11.125

Experimental method

X-RAY DIFFRACTION (2.6 Å)