Evolutionary conservation of amyloidogenic sites in the ZP polymerization domain of ZP3 homologs.

<p>Structure based sequence alignment of the ZP polymerization domain of mouse ZP3 and ZP3/egg coat homologs from <i>Haliotis rufescens</i> (red abalone) vitelline envelope receptor of lysin (VERL repeat 23), <i>Oncorhynchus mykiss</i> (rainbow trout) vitelline envelope protein gamma, <i>Xenopus laevis</i> (frog) gp41, <i>Coturnix japonica</i> (Japanese quail) glycoprotein C and human ZP3 with the amyloidogenic sites as predicted by AmylPred2 indicated by blue highlighting. The ZP-N domain in <i>Saccharomyces cerevisiae</i> α-agglutinin/Sag 1 is also shown with its predicted amyloidogenic sites. Cysteine residues are noted by black boxes. The internal hydrophobic patch (IHP) is indicated by a red box and the external hydrophobic patch (EHP) is noted by the blue box [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0129907#pone.0129907.ref035" target="_blank">35</a>]. The β-strand secondary structure based on the structure of chicken ZP3 is noted by orange bars (ZP-N subdomain) and green bars (ZP-C subdomain) [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0129907#pone.0129907.ref008" target="_blank">8</a>].