Structure and specificity of nuclear receptor-coactivator interactions.

@article{Darimont1998StructureAS,
  title={Structure and specificity of nuclear receptor-coactivator interactions.},
  author={B. Darimont and R. Wagner and J. Apriletti and M. Stallcup and P. Kushner and J. Baxter and R. Fletterick and K. Yamamoto},
  journal={Genes \& development},
  year={1998},
  volume={12 21},
  pages={
          3343-56
        }
}
Combinatorial regulation of transcription implies flexible yet precise assembly of multiprotein regulatory complexes in response to signals. Biochemical and crystallographic analyses revealed that hormone binding leads to the formation of a hydrophobic groove within the ligand binding domain (LBD) of the thyroid hormone receptor that interacts with an LxxLL motif-containing alpha-helix from GRIP1, a coactivator. Residues immediately adjacent to the motif modulate the affinity of the interaction… Expand
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