Kamada K, De Angelis J, Roeder R G, Burley S K
Laboratories of Molecular Biophysics and Biochemistry and Molecular Biology, and Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3115-20. doi: 10.1073/pnas.051631098.
The x-ray structure of a C-terminal fragment of the RAP74 subunit of human transcription factor (TF) IIF has been determined at 1.02-A resolution. The alpha/beta structure is strikingly similar to the globular domain of linker histone H5 and the DNA-binding domain of hepatocyte nuclear factor 3gamma (HNF-3gamma), making it a winged-helix protein. The surface electrostatic properties of this compact domain differ significantly from those of bona fide winged-helix transcription factors (HNF-3gamma and RFX1) and from the winged-helix domains found within the RAP30 subunit of TFIIF and the beta subunit of TFIIE. RAP74 has been shown to interact with the TFIIF-associated C-terminal domain phosphatase FCP1, and a putative phosphatase binding site has been identified within the RAP74 winged-helix domain.
已在1.02埃分辨率下测定了人类转录因子（TF）IIF的RAP74亚基C端片段的X射线结构。α/β结构与连接组蛋白H5的球状结构域以及肝细胞核因子3γ（HNF-3γ）的DNA结合结构域惊人地相似，使其成为一种翼状螺旋蛋白。这个紧凑结构域的表面静电特性与真正的翼状螺旋转录因子（HNF-3γ和RFX1）以及TFIIF的RAP30亚基和TFIIE的β亚基中的翼状螺旋结构域有显著差异。RAP74已被证明与TFIIF相关的C端结构域磷酸酶FCP1相互作用，并且在RAP74翼状螺旋结构域内已鉴定出一个假定的磷酸酶结合位点。
