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. 2014 Apr 21;9(4):e95633. doi: 10.1371/journal.pone.0095633

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This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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Superimpositions are shown between the present day consensus KoRV (Pci-SN265) protein structure and ancient KoRV variants. Amino acid variations between these sequences mapped on the protein models are shown in red and with arrows. The models are shown in cartoon ribbon representations (left panels) and as semi-transparent surfaces (right panels). The atoms of the variable amino acid residues are in line representations to view the side chains. In all comparisons the Pci-SN265 consensus was used as the reference sequence. (A) The model of the Pci-SN265 Gag protein is superimposed with the models of variants found in archival koalas um3435 and maex1738. (B) The model of the Pci-SN265 Pol protein is superimposed with variants found in QMJ6480, 582119, MCZ8574, Um3435, and maex1738. (C) The model of the Pci-SN265 Env protein is superimposed with the model of variants found in MCZ_12454 and um3435. For all three polypeptides, the structural differences predicted are attributed to changes in the polarity, charge, and atom conformations and are largely localized onto flexible loop regions.