Download MendeleyThe C-Terminal Region of the Transcriptional Regulator Thap11 Forms a Parallel Coiled-Coil Domain Involved in Protein Dimerization.
Cukier, C.D., Maveyraud, L., Saurel, O., Guillet, V., Milon, A., Gervais, V.(2016) J Struct Biol 194: 337
- PubMed: 26975212
- DOI: https://doi.org/10.1016/j.jsb.2016.03.010
- Primary Citation of Related Structures:
5AJS - PubMed Abstract:
Thanatos associated protein 11 (THAP11) is a cell cycle and cell growth regulator differentially expressed in cancer cells. THAP11 belongs to a distinct family of transcription factors recognizing specific DNA sequences via an atypical zinc finger motif and regulating diverse cellular processes. Outside the extensively characterized DNA-binding domain, THAP proteins vary in size and predicted domains, for which structural data are still lacking. We report here the crystal structure of the C-terminal region of human THAP11 protein, providing the first 3D structure of a coiled-coil motif from a THAP family member. We further investigate the stability, dynamics and oligomeric properties of the determined structure combining molecular dynamics simulations and biophysical experiments. Our results show that the C-ter region of THAP11 forms a left-handed parallel homo-dimeric coiled-coil structure possessing several unusual features.
Organizational Affiliation:
Institut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, France. Electronic address: cyprian.cukier@gmx.com.
