title: NMR studies of a new family of DNA binding proteins: the THAP proteins.
abstract: The THAP (THanatos-Associated Protein) domain is an evolutionary conserved C2CH zinc-coordinating domain shared with a large family of cellular factors (THAP proteins). Many members of the THAP family act as transcription factors that control cell proliferation, cell cycle progression, angiogenesis, apoptosis and epigenetic gene silencing. They recognize specific DNA sequences in the promoters of target genes and subsequently recruit effector proteins. Recent structural and functional studies have allowed getting better insight into the nuclear and cellular functions of some THAP members and the molecular mechanisms by which they recognize DNA. The present article reviews recent advances in the knowledge of the THAP domains structures and their interaction with DNA, with a particular focus on NMR. It provides the solution structure of the THAP domain of THAP11, a recently characterized human THAP protein with important functions in transcription and cell growth in colon cancer.
authors.affiliation: CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), 205 route de Narbonne, BP64182, 31077, Toulouse, France. virginie.gervais@ipbs.fr
authors.forename: Virginie
authors.initials: V
authors.lastname: Gervais
authors.forename: Sébastien
authors.initials: S
authors.lastname: Campagne
authors.forename: Jade
authors.initials: J
authors.lastname: Durand
authors.forename: Isabelle
authors.initials: I
authors.lastname: Muller
authors.forename: Alain
authors.initials: A
authors.lastname: Milon
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D051017:Apoptosis Regulatory Proteins / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D009687:Nuclear Proteins / Q000737:chemistry*; D054730:Protein Interaction Domains and Motifs / Q000502:physiology; D012097:Repressor Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D017386:Sequence Homology, Amino Acid
chemical_list: D051017:Apoptosis Regulatory Proteins; D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D012097:Repressor Proteins; C474080:THAP1 protein, human