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. 2002 Dec 2;21(23):6494–6504. doi: 10.1093/emboj/cdf641

graphic file with name cdf641f7.jpg

Fig. 7. Sequence alignment of death effector domains. Listed are the DEDs of mouse PEA-15 (Q62048), human FADD (Q13158), human caspase-8/FLICE (Q14790), human cellular FLIP (c-FLIP) (O15519), molluscum contagiosum virus (MCV) MC159 protein (Q98325), equine herpesvirus 2 (EHV-2) E8 protein (Q66674), human DEDD (NP_127491) and human DEDD2/FLAME3 (NP_579874). Swiss-Prot accession numbers are indicated in parentheses. The positions of helices are indicated by cylinders for PEA-15, and the helices for FADD (Eberstadt et al., 1998) are underlined. Highly conserved hydrophobic residues are shaded yellow and the conserved RxDLφ motif (x = any amino acid, φ = any hydrophobic residue) at the beginning of helix α6 is indicated by a box.