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

graphic file with name cdf641f1.jpg

Fig. 1. Three-dimensional structure of PEA-15. (A) Stereoview of the backbone atoms (N, Cα and C′) of 20 NMR conformers of PEA-15 superimposed over residues 1–97. (B) Ribbon representation of the averaged minimized structure of PEA-15. The orientation of the structure is as shown in (A). Residues 2–14, 17–27, 33–37, 42–51, 61–69 and 73–89 comprise helices α1, α2, α3, α4, α5 and α6, respectively. The helices are colored in cyan, and the loops and C-terminal tail in gray. (C) Backbone representation of the death effector domains of PEA-15 (cyan) and FADD (yellow) (Eberstadt et al., 1998; PDB accession code 1A1Z), superimposed over the Cα atoms of residues 1–83.