Figure 4
From: The IKK-binding domain of NEMO is an irregular coiled coil with a dynamic binding interface
The three hot-spot residues binding pockets. NEMO-EEAA (blue, left panels), NEMO in complex with IKKβ (PDB: 3BRV; grey, right panels), only hot-spot residues of IKKβ are shown (deep salmon). The IKKβ is shown overlaid to the NEMO-EEAA structure in transparency in the left panels for reference. (a,b) Pocket I: L708 and V709 of IKKβ in sticks. NEMO’s Glu60, Leu61, Ala 64 (top helix) and Arg62′, Ile65′, Arg66′, Asn69′ (bottom helix), also in sticks. (c,d) Pocket II: L719 and I723 of IKKβ in sticks. NEMO’s Ile71, Arg75, Glu78, Leu79 (top helix) and Leu72′, Arg75′, Cys/Ala76′, Leu79′ (bottom helix), also in sticks. (e,f), Pocket III: F734, W739 and W741 of IKKβ in sticks, NEMO’s Phe92, Leu93, Lys96, Phe99, Ala100 (top helix) and Lys90′, Leu93′, Phe97′, Ala100′, Arg101′ (bottom helix), also in sticks; (g,h) surface rendering of pocket III of NEMO-EEAA (left) and NEMO in complex with IKKβ (IKKβ removed, right). The surface area is colored by hydrophobicity red = hydrophobic, white = polar.
