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Figure 2.
Fig. 2. Structural details and sequence conservation of the
NOA motif. (a) Alignment of the NOA sequence from human, mouse,
and Drosophila NEMO homologues and from human Optineurin and
ABIN-1, -2, and -3 proteins. Numbers correspond to the first and
last residue of the protein sequence. Identical and similar
residues are colored red and yellow, respectively. Diamonds
indicate residues linked to human pathologies: EDA-ID (blue), ID
(green), and IP (red), corresponding to the following mutations
(human numbering): D311N, E315A, R319Q, and A323P. The heptad
position (a–g) is indicated at the bottom. (b) Close-up view
of the NEMO NOA region (helices are colored as in Fig. 1).
Conserved residues are shown as ball-and-stick representations,
with O and N atoms in red and blue, respectively. Broken lines
point to residues involved in salt bridge or H-bond formation.
For clarity, only one set of conserved residues is displayed.
(c) Helical wheel representation of the NOA coiled coil,
starting from residue V293 at position c. Residues linked to
human pathologies are colored red. Blue lines indicate
intermolecular salt bridges.
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