Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain.

@article{Anbanandam2006InsightsIT,
  title={Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain.},
  author={Asokan Anbanandam and Diana C. Albarado and Catherine T. Nguyen and Georg Halder and Xiaolian Gao and Sudha Veeraraghavan},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2006},
  volume={103 46},
  pages={17225-30}
}
Transcription enhancer factor 1 is essential for cardiac, skeletal, and smooth muscle development and uses its N-terminal TEA domain (TEAD) to bind M-CAT elements. Here, we present the first structure of TEAD and show that it is a three-helix bundle with a homeodomain fold. Structural data reveal how TEAD binds DNA. Using structure-function correlations, we find that the L1 loop is essential for cooperative loading of TEAD molecules on to tandemly duplicated M-CAT sites. Furthermore, using a… CONTINUE READING