Structural Studies of the PU.l Transcription Factor.
Final rept. 1 Sep 94-31 Aug 97
BURNHAM INST LA JOLLA CA
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Ets transcription factors play a role in development and are implicated in some malignant processes. Recently, members of this large gene family have been identified in normal gene expression in mammary cells and also in breast cancer cell lines. In these studies, the crystal structure of the DNA-binding domain of the PU.1 ets protein complexed to DNA has been determined at 2.1 A resolution. The DNA binding domain is a conserved region that binds the core sequence 5-GGAAT-3. The PU.1 domain binds DNA using a loop-helix-loop motif involving conserved amino acids and bases. In this project we have also used nuclear magnetic resonance NMR to determine the unbound structure of the domain in solution. The two structures were correlated to understand the process of DNA recognition by ets proteins.
- Genetic Engineering and Molecular Biology
- Medicine and Medical Research
- Nuclear Physics and Elementary Particle Physics