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Fig. 3 | BMC Genomics

Fig. 3

From: Delineating the role of c-FLIP/NEMO interaction in the CD95 network via rational design of molecular probes

Fig. 3

Homology model of NEMO/c-FLIP complex. a The homology model of c-FLIP/NEMO complex is shown. NEMO is depicted in green; DED1 and DED2 of c-FLIP are presented in orange and yellow, respectively. The sequence alignment of c-FLIP and ks-v-FLIP DED1 domains is colored according to ClustalX color scheme of Jalview software. b ks-v-FLIP/NEMO binding interface. Amino acid residues involved in interaction of ks-v-FLIP (depicted in green color) with NEMO (depicted in blue color) are shown. c c-FLIP/NEMO binding interface. Amino acid residues involved in interaction of c-FLIP (depicted in green color) with NEMO (depicted in blue color) are shown. Molecular surface is shown in gray color. For B) and C): c-FLIP and v-FLIP residues are designated at the left side of figure, while NEMO residues at the right side. Hydrogen bonds with NEMO D242 residue are shown with green dashed line

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