Fig. 5: NPC binding requires a lack of FG-repulsive residues on the capsid surface. | Nature Structural & Molecular Biology

Fig. 5: NPC binding requires a lack of FG-repulsive residues on the capsid surface.

From: Nuclear pore passage of the HIV capsid is driven by its unusual surface amino acid composition

Fig. 5

a, Targeting of conical CLPs (noncovalently filled with sinGFP4) to HeLa cell NPCs was as in Fig. 1e. Indicated mutants were tested with identical scan settings as for wild-type capsids. b, Quantification of GFP signals on NPCs. Numbers are means; bars indicate the mean ± s.d. (n = number of quantified nuclei). Statistical significance between each mutant and the wild type was determined using an unpaired Student’s t-test: ****P < 0.001. Tabular data, including P values for statistical significance of group differences, are provided in Supplementary Data 1. Scale bar, 10 μm. Experiments were independently replicated three times with consistent outcomes.

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