Observation of unphosphorylated STAT3 core protein binding to target dsDNA by PEMSA and X-ray crystallography

dc.contributor.authorNkansah, E
dc.contributor.authorShah, R
dc.contributor.authorCollie, G.W.
dc.contributor.authorParkinson, G.N.
dc.contributor.authorPalmer, J
dc.contributor.authorRahman, K.M.
dc.contributor.authorWilderspin, A.F.
dc.date.accessioned2013-06-21T13:18:35Z
dc.date.accessioned2017-10-16T11:43:51Z
dc.date.available2013-06-21T13:18:35Z
dc.date.available2017-10-16T11:43:51Z
dc.date.issued2013
dc.description.abstractThe 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 Y705en_US
dc.identifier.citationNkansah, E., Shah, R., Collie, G. W., Parkinson, G. N., Palmer, J., Rahman, K. M., . . . Wilderspin, A. F. (2013). Observation of unphosphorylated STAT3 core protein binding to target dsDNA by PEMSA and X-ray crystallography. FEBS Lettersen_US
dc.identifier.urihttp://197.255.68.203/handle/123456789/3824
dc.language.isoenen_US
dc.publisherFEBS Lettersen_US
dc.titleObservation of unphosphorylated STAT3 core protein binding to target dsDNA by PEMSA and X-ray crystallographyen_US
dc.typeArticleen_US

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