NMR studies of a new family of DNA binding proteins: the THAP proteins

被引:0
作者
Virginie Gervais
Sébastien Campagne
Jade Durand
Isabelle Muller
Alain Milon
机构
[1] IPBS (Institut de Pharmacologie et de Biologie Structurale),CNRS
[2] Université de Toulouse-UPS,IPBS
[3] ETH Zurich,undefined
来源
Journal of Biomolecular NMR | 2013年 / 56卷
关键词
DNA binding domain; THAP; NMR; Protein–DNA complex; Loop dynamics; Transcription factor; Isothermal titration calorimetry ITC; Differential scanning fluorimetry DSF; DNA binding affinity;
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学科分类号
摘要
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.
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页码:3 / 15
页数:12
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