4XB0

Structure of the Plk2 polo-box domain

Summary for 4XB0

• Entry DOI: 10.2210/pdb4xb0/pdb
• Descriptor: Serine/threonine-protein kinase PLK2, PHOSPHATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: polo-box domain, polo-like kinase 2, plk2, 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: 50489.28

Authors

Kim, J.H.,Ku, B.,Kim, S.J. (deposition date: 2014-12-16, release date: 2015-05-06, Last modification date: 2024-04-03)

Primary citation

Kim, J.H.,Ku, B.,Lee, K.S.,Kim, S.J.
Structural analysis of the polo-box domain of human Polo-like kinase 2
Proteins, 83:1201-1208, 2015

PubMed Abstract: Polo-like kinases (Plks) are the key regulators of cell cycle progression, the members of which share a kinase domain and a polo-box domain (PBD) that serves as a protein-binding module. While Plk1 is a promising target for antitumor therapy, Plk2 is regarded as a tumor suppressor even though the two Plks commonly recognize the S-pS/T-P motif through their PBD. Herein, we report the crystal structure of the PBD of Plk2 at 2.7 Å. Despite the overall structural similarity with that of Plk1 reflecting their high sequence homology, the crystal structure also contains its own features including the highly ordered loop connecting two subdomains and the absence of 310 -helices in the N-terminal region unlike the PBD of Plk1. Based on the three-dimensional structure, we furthermore could model its interaction with two types of phosphopeptides, one of which was previously screened as the optimal peptide for the PBD of Plk2.

PubMed: 25846005
DOI: 10.1002/prot.24804

Experimental method

X-RAY DIFFRACTION (2.701 Å)