Summary
PDB 4E68 deposited: 2012-03-15 modified: 2013-04-10
Title Unphosphorylated STAT3B core protein binding to dsDNA
Authors Bui, T.T., Collie, G.W., Drake, A.F., Husby, J., Neidle, S., Nkansah, E., Palmer, J., Parkinson, G.N., Rahman, K.M., Shah, R., Thurston, D.E., Wilderspin, A.F., Zinzalla, G.
Method X-RAY DIFFRACTION
Structure factors resolution 2.585 rfactor 0.22532 rfree 0.27332
DPI 0.94 theoretical min: 0.42
Citations

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.

Febs Lett. 2013 Apr; 587(7):833-839 doi:10.1016/j.febslet.2013.01.065

Cross References
Database source Identifier Description
PubMed 23434585 FEBLAL
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
4E68/1 4E68 1 tetramer 0 4 0 9048