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Crystal structure of a coiled-coil domain from human THAP11Crystal structure of a coiled-coil domain from human THAP11
Structural highlights
FunctionTHA11_HUMAN Transcriptional repressor that plays a central role for embryogenesis and the pluripotency of embryonic stem (ES) cells. Sequence-specific DNA-binding factor that represses gene expression in pluripotent ES cells by directly binding to key genetic loci and recruiting epigenetic modifiers (By similarity). Publication Abstract from PubMedThanatos 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. References
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