Figure 3
From: DED or alive: assembly and regulation of the death effector domain complexes
Conserved features of the DED protein family. (a) Homology model of the tandem DEDs of human FLIP (orange ribbon) depicting the main conserved residues part of the hydrophobic patch (highlighted in grey), which are essential for inter- and intra-DED–DED interactions. (b) Sequence alignment of residues that form part of the hydrophobic patches, which are highly conserved amongst DED proteins. (c) Homology model of human FLIP DEDs (orange ribbon) with a close-up view of the two E/D-RxDL motifs. Only residues that form the charged triad motifs (highlighted in cyan) are shown. Hydrogen bonds are highlighted in black dotted lines. (d) Sequence alignment of the E/D-RxDL motifs which are conserved amongst DED proteins
