Sequence alignments between host and pathogen CYP51.

<p>Sequence alignments between CYP51 from <i>Trypanosoma cruzi</i>, <i>Trypanosoma brucei, Aspergillus fumigatus</i>, <i>Candida albicans</i> and human. Accession numbers of the proteins in the Swiss-Prot/TrEMBL (<a href="http://us.expasy.org/sprot" target="_blank">http://us.expasy.org/sprot</a>) and NCBI (<a href="http://www.ncbi.nlm.nih.gov/" target="_blank">http://www.ncbi.nlm.nih.gov/</a>) databases are given next to the name of the protein. Alignments were performed using CLUSTALW program online <a href="http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0000651#pntd.0000651-Thompson1" target="_blank">[61]</a>. The figure was generated using ESPript <a href="http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0000651#pntd.0000651-Gouet1" target="_blank">[62]</a>. The secondary structure annotation and residue numbering at the top correspond to CYP51_Tc, residue numbering at the bottom corresponds to human CYP51. The α-helices are labeled with capital letters according to generally accepted P450 nomenclature. The β-strands of large β-sheets are labeled with dashed numbers. Sequential numbers are used to label short two-residue β-strands. Residues within 7 Å of fluconazole are labeled with blue triangles. Additional residues constituting the hydrophobic tunnel are labeled with green triangles. Human H236 and H489 and the corresponding residues in the pathogenic species are highlighted in yellow. Residues corresponding to CYP51_Tc I105 are highlighted in cyan. Mutation hot spots at the tunnel opening are marked with black stars. Gray stars highlight residues in alternate conformations.