Crystal structure of unphosphorylated STAT3 core fragment.

@article{Ren2008CrystalSO,
  title={Crystal structure of unphosphorylated STAT3 core fragment.},
  author={Zhiyong Ren and Xiang Mao and Claudia Mertens and R KrishnaRaj and Jie Qin and Pijus Kumar Mandal and Michael J. Romanowski and John S. McMurray and Xiaomin Chen},
  journal={Biochemical and biophysical research communications},
  year={2008},
  volume={374 1},
  pages={
          1-5
        }
}
Signal transducers and activators of transcription (STATs) are latent cytoplasmic transcriptional factors that play an important role in cytokine and growth factor signaling. Here we report a 3.05 A-resolution crystal structure of an unphosphorylated STAT3 core fragment. The overall monomeric structure is very similar to that of the phosphorylated STAT3 core fragment. However, the dimer interface observed in the unphosphorylated STAT1 core fragment structure is absent in the STAT3 structure… CONTINUE READING
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