| First Author | Fribourg S | Year | 2000 |
| Journal | J Biol Chem | Volume | 275 |
| Issue | 41 | Pages | 31963-71 |
| PubMed ID | 10882739 | Mgi Jnum | J:65131 |
| Mgi Id | MGI:1891809 | Doi | 10.1074/jbc.M004960200 |
| Citation | Fribourg S, et al. (2000) Structural characterization of the cysteine-rich domain of TFIIH p44 subunit. J Biol Chem 275(41):31963-71 |
| abstractText | 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. |
