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Science 24 January 1992:
Vol. 255. no. 5043, pp. 464 - 466
DOI: 10.1126/science.1734524
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Articles

Science, Vol 255, Issue 5043, 464-466
Copyright © 1992 by American Association for the Advancement of Science

articles

Predicted structural similarities of the DNA binding domains of c-Myc and endonuclease Eco RI

TD Halazonetis and AN Kandil

Department of Cancer Research, Merck Sharp and Dohme Research Laboratories, West Point, PA 19486.

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.


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Identification and Characterization of Specific DNA-binding Complexes Containing Members of the Myc/Max/Mad Network of Transcriptional Regulators.
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