人转录因子IIF的RAP74亚基C末端结构域的晶体结构
Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF.
作者信息
Kamada K, De Angelis J, Roeder R G, Burley S K
机构信息
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.
出版信息
Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3115-20. doi: 10.1073/pnas.051631098.
Abstract
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.
摘要
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。
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