2jnj: Difference between revisions
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'''Solution structure of the p8 TFIIH subunit''' | '''Solution structure of the p8 TFIIH subunit''' | ||
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[[Category: Poterszman, A.]] | [[Category: Poterszman, A.]] | ||
[[Category: Vitorino, M.]] | [[Category: Vitorino, M.]] | ||
[[Category: | [[Category: Protein]] | ||
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Revision as of 06:04, 4 May 2008
Solution structure of the p8 TFIIH subunit
Overview
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.
About this Structure
2JNJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy., Vitorino M, Coin F, Zlobinskaya O, Atkinson RA, Moras D, Egly JM, Poterszman A, Kieffer B, J Mol Biol. 2007 Apr 27;368(2):473-80. Epub 2007 Feb 20. PMID:17350038 Page seeded by OCA on Sun May 4 09:04:35 2008
