Crystal structure of MyoD bHLH domain-DNA complex: Perspectives on DNA recognition and implications for transcriptional activation

@article{Ma1994CrystalSO,
  title={Crystal structure of MyoD bHLH domain-DNA complex: Perspectives on DNA recognition and implications for transcriptional activation},
  author={P. C. Ma and M. A. Rould and H. Weintraub and C. Pabo},
  journal={Cell},
  year={1994},
  volume={77},
  pages={451-459}
}
  • P. C. Ma, M. A. Rould, +1 author C. Pabo
  • Published 1994
  • Biology, Medicine
  • Cell
  • The crystal structure of a MyoD basic-helix-loop-helix (bHLH) domain-DNA complex has been solved and refined at 2.8 A resolution. This structure proves that bHLH and bHLH-leucine zipper (bHLH-ZIP) proteins are remarkably similar; it helps us understand subtle differences in binding preferences for these proteins; and it has surprising implications for our understanding of transcription. Specifically, Ala-114 and Thr-115, which are required for positive control in the myogenic proteins, are… CONTINUE READING
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