Fig. 6: Comparisons of the 10–1074 and 8ANC195 binding interfaces formed with CRF01_AE_ T/F100 SOSIP.664 wild type and its LMHS mutant unbound or bound to temsavir. | Nature Communications

Fig. 6: Comparisons of the 10–1074 and 8ANC195 binding interfaces formed with CRF01_AE_ T/F100 SOSIP.664 wild type and its LMHS mutant unbound or bound to temsavir.

From: Structure-function analyses reveal key molecular determinants of HIV-1 CRF01_AE resistance to the entry inhibitor temsavir

Fig. 6

a, c Buried Surface Area (BSA) contributed by individual residues of Env and the Fabs of 10–1074 (c) and 8ANC195 (b) in apo CRF01_AE_ T/F100 LMHS SOSIP.664 and CRF01_AE_ T/F100 LMHS SOSIP.664 bound to temsavir. The total Env glycan contribution to the interface is shown as a separate bar with the value of BSA shown at the top. BSA values represent the average of the three copies in the trimer. b Superimposition of the complexes with 10–1074 and 8ANC195 colored green, yellow and gray for wild-type CRF01_AE_ T/F100 SOSIP.664, and its apo and temsavir-bound LMHS mutant complexes, respectively. Blow-ups show similarities/differences between the complexes of how individual Fab/antibody residues interact with the Env antigen.

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