@article{87766,
  keywords = {Models, Molecular, Protein Structure, Tertiary, Humans, Crystallization, Molecular Sequence Data, Amino Acid Sequence, Cell Transformation, Viral, Simian virus 40, Electrophoresis, Polyacrylamide Gel, Protein Subunits, Protein Phosphatase 2, Antigens, Viral, Tumor},
  author = {Yu Chen and Yanhui Xu and Qing Bao and Yongna Xing and Zhu Li and Zheng Lin and Jeffry Stock and Philip Jeffrey and Yigong Shi},
  title = {Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40.},
  abstract = { The small t antigen (ST) of DNA tumor virus SV40 facilitates cellular transformation by disrupting the functions of protein phosphatase 2A (PP2A) through a poorly defined mechanism. The crystal structure of the core domain of SV40 ST bound to the scaffolding subunit of human PP2A reveals that the ST core domain has a novel zinc-binding fold and interacts with the conserved ridge of HEAT repeats 3-6, which overlaps with the binding site for the B{\textquoteright} (also called PR61 or B56) regulatory subunit. ST has a lower binding affinity than B{\textquoteright} for the PP2A core enzyme. Consequently, ST does not efficiently displace B{\textquoteright} from PP2A holoenzymes in vitro. Notably, ST inhibits PP2A phosphatase activity through its N-terminal J domain. These findings suggest that ST may function mainly by inhibiting the phosphatase activity of the PP2A core enzyme, and to a lesser extent by modulating assembly of the PP2A holoenzymes. },
  year = {2007},
  journal = {Nat Struct Mol Biol},
  volume = {14},
  pages = {527-34},
  month = {06/2007},
  issn = {1545-9993},
  doi = {10.1038/nsmb1254},
  language = {eng},
}