Fig. 5: Assembly of active MLKL tetramer requires interactions mediated by three domains.
From: Phosphorylation-dependent pseudokinase domain dimerization drives full-length MLKL oligomerization
a–c MLKL tetramerization interface residues (sticks) whose mutation disrupted necroptosis mapped on the model of full-length human MLKL tetramer (mutants reported by previous studies40,47,52 are labelled with asterisks). a Four-helix bundle (4HB) domain tetramerization interface (top-down view); b brace helix coiled coil; c pseudokinase domain dimerization interface (zoomed panel shows the phosphorylated (p)-MLKL pseudokinase domain crystal structure, PDB: 8SLZ). d Proposed mechanism by which RIPK3-mediated phosphorylation drives MLKL tetramerization and cell death during necroptosis. The skull and crossbones image (Mycomorphbox_Deadly.png; by Sven Manguard) was used under a Creative Commons Attribution-Share Alike 4.0 license.
