Figure 5
From: Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V
HeV V adopts a more compact conformation upon exportin-1/RanGTP or importin α2/β1 binding as determined by SAXS analysis. (a) Size exclusion chromatography profiles for the V:exportin-1/Ran-GTP SAXS experiment. Rg values of HeV V, exportin-1/Ran-GTP and the V:exportin-1/Ran-GTP complex were calculated across each peak, with average values of 72.0 ± 0.5 Å, 44.0 ± 0.6 Å and 64 ± 0.2 Å, respectively, shown by horizontal lines. (b) Size exclusion chromatography profiles for the V:importin α2/β1 SAXS experiment. Radius of gyration (Rg) values of HeV V, importin α2/β1 and the V:importin α2/β1 complex were calculated across each peak, with average values of 72.0 ± 0.5 Å, 52.0 ± 0.7 Å and 85.0 ± 0.6 Å, respectively, shown by horizontal lines. (c) P(r) plots for HeV V, exportin-1/Ran-GTP and the V:exportin-1/Ran-GTP complex. (d) P(r) plots for HeV V, importin α2/β1 and the V:importin α2/β1 complex. Kratky plots show that unlike (e) exportin-1/Ran-GTP and (f) importin α2/β1, V shows no globular fold. Some lack of structure is retained in the V:exportin-1/Ran-GTP and V:importin α2/β1 complexes.
