Extended Data Fig. 6: Reduction of FG phase-solubility by FG-repulsive capsid mutations depends on the accessibility of the mutated residues.
From: Nuclear pore passage of the HIV capsid is driven by its unusual surface amino acid composition
a, The FG phase-partitioning of CLPs was tested as in Fig. 3, using wild-type and indicated mutants. Partitioning was strongly inhibited by FG-repulsive mutations at highly accessible residues (A92E and R97K). When similar mutations were introduced at less accessible positions, partitioning was little affected (R132K) or unaffected (L136E or R143K). Experiments were independently replicated three times with consistent outcomes. b, A92, R97, R132, L136 and R143 are shown with indicated coloring in a capsid structure (PDB 3J3Y).
