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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Structural characterization of the cysteine-rich domain of TFIIH p44 subunit.

In an effort to understand the structure function relationship of TFIIH, a transcription/repair factor, we focused our attention on the p44 subunit, which plays a central role in both mechanisms. The amino-terminal portion of p44 has been shown to be involved in the regulation of the XPD helicase activity; here we show that its carboxyl-terminal domain is essential for TFIIH transcription activity and that it binds three zinc atoms through two independent modules. The first contains a C4 zinc finger motif, whereas the second is characterized by a CX(2)CX(2-4)FCADCD motif, corresponding to interleaved zinc binding sites. The solution structure of this second module reveals an unexpected homology with the regulatory domain of protein kinase C and provides a framework to study its role at the molecular level.[1]

References

  1. Structural characterization of the cysteine-rich domain of TFIIH p44 subunit. Fribourg, S., Kellenberger, E., Rogniaux, H., Poterszman, A., Van Dorsselaer, A., Thierry, J.C., Egly, J.M., Moras, D., Kieffer, B. J. Biol. Chem. (2000) [Pubmed]
 
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