Predicted structural similarities of the DNA binding domains of c-Myc and endonuclease Eco RI.
The c-Myc oncoprotein belongs to a family of proteins whose DNA binding domains contain a basic region-helix-loop-helix (bHLH) motif. Systematic mutagenesis of c-Myc revealed that dimerized bHLH motifs formed a parallel four-helix bundle with the amino termini of helices 1 and 2 directed toward the inner and outer nucleotides of the DNA binding site, respectively. Both the basic region and the carboxyl-terminal end of the loop contributed to DNA binding specificity. The DNA binding domain of c-Myc may therefore be structurally similar to that of restriction endonuclease Eco RI.
Halazonetis
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Department of Cancer Research, Merck Sharp and Dohme Research Laboratories, West Point, PA 19486.
Kandil
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D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry*; D015246:Deoxyribonuclease EcoRI / Q000737:chemistry*; D006801:Humans; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D016271:Proto-Oncogene Proteins c-myc / Q000737:chemistry*; D016415:Sequence Alignment; D014157:Transcription Factors / Q000737:chemistry
D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D016271:Proto-Oncogene Proteins c-myc; D014157:Transcription Factors; D015246:Deoxyribonuclease EcoRI