This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.NMR studies to determine the mechanism of binding of the antiviral and anticancer agent P4N to the DNA cognate site of the transcription factor Sp1. P4N (a derivative of the plant ligand nordihydroguaiaretic acid, NDGA) inhibits Sp1-DNA interaction by competing directly with Sp1 for the same DNA-binding site. We apply NMR to study at molecular level the different modes of binding of the drug P4N and the structural perturbation of the DNA upon P4N binding.
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