Alignment of the bHLHZip domains of c-MYC and MYCN.

<p>The amino acids in the bHLHZip domains of human c-MYC and human MYCN were aligned, while the secondary structure is indicated above. Identical amino acid are denoted (*), conserved substitution (:) and semi-conserved substitution (.). The two binding sites for the specified compounds as reported by Hammoudeh <i>et al</i> is indicated by a colored square <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0097285#pone.0097285-Hammoudeh1" target="_blank">[38]</a>. Each small molecule is positioned under their reported or assumed binding site <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0097285#pone.0097285-Hammoudeh1" target="_blank">[38]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0097285#pone.0097285-Wang1" target="_blank">[39]</a>. For the 10058-F4 analogs #474 and #764 as well as its potential metabolite C-<i>m/z</i> 232 the binding sites have not been determined experimentally <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0097285#pone.0097285-Wang1" target="_blank">[39]</a>. Through the similarity of their chemical structure to 10058-F4, it has been assumed that these compounds bind to the same site as indicated.