Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain.

@article{Razeto2004StructureOT,
  title={Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain.},
  author={Adelia Razeto and Venkatesh Ramakrishnan and Claudia M Litterst and Karin Giller and Christian Griesinger and Teresa Carlomagno and Nils A. Lakomek and Thomas Heimburg and Marco Lodrini and Edith B Pfitzner and Stefan Becker},
  journal={Journal of molecular biology},
  year={2004},
  volume={336 2},
  pages={319-29}
}
Signal transducer and activator of transcription 6 (STAT6) regulates transcriptional activation in response to interleukin-4 (IL-4) by direct interaction with coactivators. The CREB-binding protein (p300/CBP) and the nuclear coactivator 1 (NCoA-1), a member of the p160/steroid receptor coactivator family, bind independently to specific regions of the STAT6 transactivation domain and act as coactivators. The interaction between STAT6 and NCoA-1 is mediated by an LXXLL motif in the… CONTINUE READING
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