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X-ray crystallographic studies of eukaryotic transcription factors.

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  • 1Laboratories of Molecular Biophysics, Rockefeller University, New York, New York 10021-6399.


Our X-ray crystallographic work on eukaryotic transcription factors traverses the entire length of a typical class II nuclear gene promoter, including the TATA-box-binding protein, two b/HLH/Z promoter proximal binding factors (Max and USF), and an enhancer-binding factor (HNF-3 gamma). These high-resolution studies of specific protein/DNA interactions will be extended to include homologous proteins complexed with similar oligonucleotides and a systematic examination of the roles of individual amino acids and bases implicated in specific DNA binding. In the longer term, we will turn our attention to the myriad of protein/protein interactions occurring within TFIID and the PIC, and between the PIC and factors binding to promoter proximal and distal enhancer elements.

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