| First Author | Nkansah E | Year | 2013 |
| Journal | FEBS Lett | Volume | 587 |
| Issue | 7 | Pages | 833-9 |
| PubMed ID | 23434585 | Mgi Jnum | J:245300 |
| Mgi Id | MGI:5916841 | Doi | 10.1016/j.febslet.2013.01.065 |
| Citation | Nkansah E, et al. (2013) Observation of unphosphorylated STAT3 core protein binding to target dsDNA by PEMSA and X-ray crystallography. FEBS Lett 587(7):833-9 |
| abstractText | The STAT3 transcription factor plays a central role in a wide range of cancer types where it is over-expressed. Previously, phosphorylation of this protein was thought to be a prerequisite for direct binding to DNA. However, we have now shown complete binding of a purified unphosphorylated STAT3 (uSTAT3) core directly to M67 DNA, the high affinity STAT3 target DNA sequence, by a protein electrophoretic mobility shift assay (PEMSA). Binding to M67 DNA was inhibited by addition of increasing concentrations of a phosphotyrosyl peptide. X-ray crystallography demonstrates one mode of binding that is similar to that known for the STAT3 core phosphorylated at Y705. |
