Extended Data Fig. 8: Effect of Vif–CBFβ–A3FCTDm complex on A3FCTDm deaminase activity.
From: Structural basis of antagonism of human APOBEC3F by HIV-1 Vif
a, UDG-based deamination assay of A3FCTDm (+: 5 μM; 15×: 75 μM) in the presence or absence of different molar excesses (2×: 10 μM; 30×: 150 μM; 40×: 200 μM) of MBP-tagged Vif–CBFβ–EloB–EloC variants. The inhibition of A3FCTDm deamination activity by a large excess of Vif–CBFβ–EloB–EloC variants was not caused by nonspecific binding interactions, as the same molar amount excess (40×) of BSA did not trigger the inhibition. b, One of the Vif–CBFβ–A3FCTDm tetramer interface involving the 55VxIPLx4-5L64 motif (Extended Data Fig. 4a, left) blocks the catalytic site of A3FCTDm (red and marked by an arrow). Vif is shown in magenta, CBFβ in cyan, and A3FCTDm in green. One Vif–CBFβ–A3FCTDm ternary complex with the major interface is circled with an oval.
