Figure 3
From: The IKK-binding domain of NEMO is an irregular coiled coil with a dynamic binding interface
The structure of unbound NEMO is an irregular coiled coil. (a) The NEMO-EEAA dimer is shown as a ribbon, light blue = coiled-coil adaptors, blue = NEMO (51–112). a (hot pink) and d (blue) residues are shown in spheres. Residues in the discontinuity region (73–90) are not shown (except Leu79). (b) Sequence alignment of NEMO and NEMO-EEAA, the coiled-coil adaptors sequence is underlined and the mutations are highlighted in pink; the heptad repeats are marked under the sequence: the region with low coiled-coil propensity is in bold and the stutter region is in blue. (c,d) Effect of the stutter on core residue packing: the Cα of a and d residues are shown, coloring as in (a): (c) ideal coiled-coil region of NEMO (23–57), left, compared to the irregular region of NEMO (69–103), right. (d) the core packing is disrupted in the discontinuities region, shown the dimer of NEMO (72–92) with side chains of a and d residues in sticks (coloring as in (a)). (e) Superposition of apo NEMO-EEAA structure (blue) and NEMO (44–111) from the IKKβ-bound structure (grey, PDB: 3BRV, IKKβ is not displayed), shown as ribbons; the structures are aligned on chain A, region 44–111 only.
