Structural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions
Fig 2
NMR-monitored titrations of KAHRP with spectrin.
(A,B) Overlays of regions from 13C-HSQC NMR spectra of 50 μM of 13C-labeled KAHRP K2 alone (red) and in the presence (blue) of 150 μM unlabeled spectrin β10–14 (A) or α12–16 (B). Spectra were recorded at 10°C. Panels i and ii in the middle present magnifications of areas from the panels A and B, respectively. (C) The relative intensity of all discrete NMR peaks corresponding to Cα atoms of KAHRP K2 in the presence of β10–14 (top) or α12–16 (bottom), derived from panels A and B, respectively. Reduction of peak intensities suggests association between proteins. Error bars correspond to one standard deviation and derive from the signal / noise ratio of spectra.