Author: Nkansah, Edwin; Shah, Rahi; Collie, Gavin W.; Parkinson, Gary N.; Palmer, Jonathan; Rahman, Khondaker M.; Bui, Tam T.; Drake, Alex F.; Husby, Jarmila; Neidle, Stephen; Zinzalla, Giovanna; Thurston, David E.; Wilderspin, Andrew F.
Description: 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.
Subject headings: Animals; Binding Sites; Binding, Competitive; Circular Dichroism; Crystallography; X-Ray; DNA; Electrophoretic Mobility Shift Assay; Humans; Luminescent Proteins; Models, Molecular; Nucleic Acid Conformation; Phosphopeptides; Phosphorylation; Protein Binding; Protein Structure; Secondary, Protein Structure; Tertiary; STAT3 Transcription Factor; Tyrosine
Publication year: 2013
Journal or book title: FEBS Letters
Volume: 587
Issue: 7
Pages: 833-839
Find the full text: https://www.sciencedirect.com/science/article/pii/S0014579313001105
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Serial number: 3830