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

Cell. 1994 May 6;77(3):451-9. doi: 10.1016/0092-8674(94)90159-7.


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 buried at the protein-DNA interface. These residues are not available for direct protein-protein contacts, but they may determine the conformation of Arg-111. Comparisons with Max suggest that the conformation of this arginine, which is different in the two structures, may play an important role in myogenic transcription.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Basic-Leucine Zipper Transcription Factors
  • Binding Sites
  • Computer Graphics
  • Crystallization
  • Crystallography, X-Ray
  • DNA-Binding Proteins / chemistry
  • Helix-Loop-Helix Motifs*
  • Models, Molecular
  • Molecular Sequence Data
  • MyoD Protein / chemistry*
  • MyoD Protein / genetics
  • MyoD Protein / metabolism
  • Nucleic Acid Conformation
  • Peptides / chemical synthesis
  • Peptides / isolation & purification
  • Polynucleotides / chemical synthesis
  • Polynucleotides / metabolism*
  • Protein Conformation*
  • Sequence Alignment
  • Transcription Factors*


  • Basic-Leucine Zipper Transcription Factors
  • DNA-Binding Proteins
  • Myc associated factor X
  • MyoD Protein
  • Peptides
  • Polynucleotides
  • Transcription Factors