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• W1994847716 abstract "Trichothiodystrophy (TTD) is a rare hereditary multi-system disorder associated with defects in nucleotide excision repair (NER) and transcription as consequences of mutations in XPB, XPD and p8/TTD-A subunits of transcription factor IIH (TFIIH). Here, we report the solution structure of the p8/TTD-A protein, a small alpha/beta protein built around an antiparallel beta-sheet that forms a homodimer with an extended interface. In order to characterize the dimer interface, we have introduced a mutation at position 44, which destabilizes the dimeric form of the protein. We have shown that this mutation has no effect on the intrinsic ability of p8/TTD-A to stimulate NER in vitro, but affects the capacity of p8/TTD-A to restore TFIIH concentration in TTD-A fibroblasts. Point mutations found in TTD-A patients are discussed on the basis of the present structure." @default.
• W1994847716 created "2016-06-24" @default.
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• W1994847716 date "2007-04-01" @default.
• W1994847716 modified "2023-10-16" @default.
• W1994847716 title "Solution Structure and Self-association Properties of the p8 TFIIH Subunit Responsible for Trichothiodystrophy" @default.
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• W1994847716 doi "https://doi.org/10.1016/j.jmb.2007.02.020" @default.
• W1994847716 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17350038" @default.
• W1994847716 hasPublicationYear "2007" @default.
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