Sequence conservation and model structure of Bos1 HAMP domains.

<p>The amino-acid sequences of the six HAMP domains of the Bos1 protein were aligned with Clustal W. Amino acids identical over 80% are in bold. In the bottom panel “*” denotes hydrophobic core residues at critical heptad positions and hydrophobic residues of the connector. “g” corresponds to the conserved glycine residues of the connector motif (according to <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0042520#pone.0042520-Airola1" target="_blank">[35]</a> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0042520#pone.0042520-Parkinson1" target="_blank">[32]</a>). Interacting residues derived from <i>in silico</i> structures are highlighted in yellow. Mutated residues are shaded with the following color code according to the phenotypes indicated in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0042520#pone-0042520-t003" target="_blank">Table 3</a>: red = HR to iprodione and phenylpyrroles, osmosensitivity; green = LR to iprodione; purple = MR to iprodione and osmosensitivity. The structure of the HAMP domain 3 was predicted on the SWISS-MODEL server using the alignment mode (for details see text). Portions of the HAMP sequences involved in the typical HAMP structures AS1, AS2 and the connector are indicated above the sequence.