Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5913618 | Journal of Structural Biology | 2016 | 27 Pages |
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.
Keywords
HBMOligomerizationSEChetNOEIPTGDTTRMSDisopropyl-β-d-1-thiogalactopyranosideIMACCSIroot-mean-square deviationTHAPTevTractNMRDissociation constantMolecular dynamicsdithiothreitolCrystal structurechemical shift indexLuria–BertaniMALSTobacco etch virusMultiangle light scatteringSize exclusion chromatographyimmobilized metal affinity chromatographyCoiled-coil
Related Topics
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Molecular Biology
Authors
Cyprian D. Cukier, Laurent Maveyraud, Olivier Saurel, Valérie Guillet, Alain Milon, Virginie Gervais,