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. 2018 Jul 28;46(19):10368–10379. doi: 10.1093/nar/gky676

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 6. — A view of the Vif-interaction interface in the cpzA3H dimer. (A) Two separate A3H sites are responsible for Vif binding. cpzA3H and dsRNA are represented in gray ribbons with a transparent surface and orange/yellow ribbons with nucleobases, respectively. The residues (magenta sticks) critical for HIV-1–Vif interaction are mapped on the dimer structure. (B) Highlighted view of the Vif-binding interface and its unique residue Q97 in the chimpanzee-bonobo lineage. Residue Q97 is one of the most important determinants for the differential sensitivity of HIV-1/SIVcpz Vifs. A putative path for the extended ssRNA portion is also shown (orange dashed line).