투고논문

Structural characterization of the putative DNA-binding domain of CP2c and its relevance to zinc binding

2 College of Pharmacy and Gachon Institute of Pharmaceutical Sciences, Gachon University, Incheon 21936, Republic of Korea

3 Protein Structure Group, Korea Basic Science Institute, Ochang, Chungbuk 28119, Republic of Korea

4 Department of Life Science and Research Institute for Natural Sciences, College of Natural Sciences, Hanyang University, Seoul 04763, Republic of Korea

The transcription factor CP2c has been recently validated as an oncogenic protein that can serve as a promising target for anticancer therapy. We have recently documented that a recombinant protein corresponding to the putative DNA-binding region (residues 63-244) of CP2c adopted two different conformers, one of which is dominated by zinc binding. However, in the present study, a longer construct encompassing residues 63-302 appeared to form a single structural domain. This domain could be considered to adopt a functionally relevant fold, as the known specific binding of a dodecapeptide to this protein was evident. Hence, the residues 63-302 region rather than 63-244 can be regarded as a natively folded structural domain of CP2c. In addition, it was confirmed that zinc ions can bind to this putative DNA-binding domain of CP2c, which resulted in reduced stability of the protein. In this context, it is suggested that the mode of action of CP2c would resemble that of tumor suppressor p53.

*Address correspondence to: Hyung-Sik Won, Department of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungju-si, Chungbuk-do 27478, Republic of Korea, Tel: 82-43-840-3589, E-mail: wonhs@kku.ac.kr