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. 2017 Aug 9;5:169. doi: 10.3389/fped.2017.00169

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Copyright © 2017 Taghdiri, Dastsooz, Fardaei, Mohammadi, Farazi Fard and Faghihi.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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(A) By using I-Mutant v2.0, it was revealed that with the substitution from Glu 374 to Asp, the stability of the protein will be decreased. (B) All alterations of stability for all other amino acids in this residue were also predicted by this program. As can be seen, most of the substitutions in this region can decrease the stability of the protein. (C) Comparative amino acids alignment of ERCC8 protein across Kingdoms shows that the Glu374 residue is highly conserved during evolution. The conserved Glu (E) residue is shown in the rectangular box. Protein sequences were obtained from National Center for Biotechnology. Symbols: (*)—identical amino acids; (:)—just similar amino acids.