BioDesign 2021; 9(4): 63-66
Published online December 30, 2021
© Korean Society for Structural Biology
Dahwan Lim1,2, Chang Hoon Lee3, Ho-Chul Shin1, Seung Jun Kim1,* and Bonsu Ku1,*
1Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Republic of Korea
2Department of Biochemistry, Chungnam National University, Daejeon 34134, Republic of Korea
3Center for Information-Based Drug Research, Korea Research Institute of Chemical Technology, Daejeon 34114, Republic of Korea
A tumor suppressor protein PTPN14 interacts with the oncoprotein E7 of human papillomaviruses, leading to its proteasomal degradation. Introduction of F1044S, G1055Q, and E1095A mutations into its phosphatase domain restored the antitumor activity by impairing the interaction with E7, showing the therapeutic potential of this mutant form against human papillomavirus-involved cancers. In this study, the phosphatase domain of PTPN14 containing the three mutations was produced in an Escherichia coli expression system, purified using Ni-NTA affinity and size exclusion chromatographies, and then crystallized. X-ray diffraction data with a maximum resolution of 1.50 Å were successfully collected, and a preliminary diffraction analysis was conducted. Our crystals belonged to the P21 space group with unit cell parameters of a = 43.9 Å, b = 74.3 Å, c = 47.8 Å, and β = 102.0°. The asymmetric unit contains one protein molecule with a 45% solvent content and a 2.2 Å3/Da Matthews coefficient.