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. 2020 Nov 17;10(11):1564. doi: 10.3390/biom10111564

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Modeling of T. cruzi PS as a multi-pass transmembrane protein. The model is based on the predictive results obtained using TopCons (https://topcons.net/pred), and layout was generated using Protter (http://wlab.ethz.ch/protter/). The model with 9 transmembrane domains reveals all 11 identified epitopes, probable sites of endoproteolytic cleavage (arrow), and the localization of the typical domains listed in Table 2. (*) Highly conserved domain in the PS-like catalytic pocket (YD and GLGD).