5ajs

Publication Abstract from PubMed

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.

The C-terminal region of the transcriptional regulator THAP11 forms a parallel coiled-coil domain involved in protein dimerization.,Cukier CD, Maveyraud L, Saurel O, Guillet V, Milon A, Gervais V J Struct Biol. 2016 Jun;194(3):337-46. doi: 10.1016/j.jsb.2016.03.010. Epub 2016 , Mar 11. PMID:26975212^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.