Figure 5 | Scientific Reports

Figure 5

From: Deviated binding of anti-HBV nucleoside analog E-CFCP-TP to the reverse transcriptase active site attenuates the effect of drug-resistant mutations

Figure 5The alternative text for this image may have been generated using AI.

Deviated binding of E-CFCP-TP. (a) Superimposition of bound E-CFCP-TP, ETV-TP, and dGTP reported in this study. The location of β2–β3 strands is indicated by the arrow. (b) Schematic diagram showing the binding position and orientation of the five-membered ring moiety of E-CFCP-TP, ETV-TP, and dGTP. Deviated binding of E-CFCP-TP is indicated by red arrows. The pushing of Met184 by methylene/fluoromethylene is indicated by blue arrows. (c) Structural effect of drug-resistant M184V mutation on exocyclic methylene (ETV) and fluoromethylene (E-CFCP-TP). A severe steric clash is expected to occur between the methylene of ETV and the Val184 sidechain, while the fluorine of E-CFCP is expected to be located relatively distant from the Val184 sidechain. (d) Deviated binding mode of bound dCTP in RT3MB/M184V/F160M22 and E-CFCP-TP in RT3MB colored blue and magenta, respectively. Bound ETV-TP and dGTP in HIV-1RT3MB are also shown in yellow and gray, respectively. As shown here, the C1′ and C2′ of the bound dCTP occupy the same position as those of E-CFCP-TP.

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