Fig. 4 | Nature Communications

Fig. 4

From: Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis

Fig. 4

hMLKL(2–471) liposome permeabilization activity is affected by PsK domain mutations that disrupt the molecular switch. a Residues mutated in the present study are shown as sticks on the E351K hMLKL model generated in the course of this study (Fig. 2a), with zoomed views of the 4HB-PsK interface (panel 1) and the pseudoactive site in the PsK domain (panel 2) shown on the right. b–l 5(6)-Carboxyfluorescein egress from liposomes induced by 1 μM full-length hMLKL in the presence (red) and absence (blue) of 500 μM ATP was monitored by absorbance at 485 nm for K16A/R17A (b), K354A/T355A (c), K230M (d), E258K (e), G330E (f), E258K/E351K (g), T357E/S358E (h), T357E/S358E/E351K (i), K255A/K256A (j), D107A/E111A (k), and K157A (l) mutants. Data represent mean ± SEM of three independent assays

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