1pfj
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(New page: 200px<br /> <applet load="1pfj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pfj" /> '''Solution structure of the N-terminal PH/PTB...)
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Revision as of 16:36, 12 November 2007
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Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit
Overview
The human general transcription factor TFIIH is involved in both, transcription and DNA repair. We have identified a structural domain in, the core subunit of TFIIH, p62, which is absolutely required for DNA, repair activity through the nucleotide excision repair pathway. Using, coimmunoprecipitation experiments, we showed that this activity involves, the interaction between the N-terminal domain of p62 and the 3', endonuclease XPG, a major component of the nucleotide excision repair, machinery. Furthermore, we reconstituted a functional TFIIH particle with, a mutant of p62 lacking the N-terminal domain, showing that this domain is, not required for assembly of the TFIIH complex and basal transcription. We, solved its three-dimensional structure and found an unpredicted pleckstrin, homology and phosphotyrosine binding (PH/PTB) domain, uncovering a new, class of activity for this fold.
About this Structure
1PFJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
TFIIH contains a PH domain involved in DNA nucleotide excision repair., Gervais V, Lamour V, Jawhari A, Frindel F, Wasielewski E, Dubaele S, Egly JM, Thierry JC, Kieffer B, Poterszman A, Nat Struct Mol Biol. 2004 Jul;11(7):616-22. Epub 2004 Jun 13. PMID:15195146
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