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Figure 3.
Figure 3. Structure of NEMO[CoZi] in Complex with Diubiquitin
(A and B) Overall structure of the NEMO[CoZi]●diubiquitin
complex in two orthogonal views. The two chains of NEMO are
colored in green and violet; Ub[distal] is shown in orange, and
Ub[proximal] in gold.
(C and D) Open-book representation of
NEMO UBAN motif recognition of distal and proximal ubiquitin
moities. In (C), residues from Ub[distal] (orange) and
Ub[proximal] (gold) that interact with the NEMO UBAN motif are
labeled on the diubiquitin surface, indicating two mutually
exclusive binding surfaces. (D) shows a surface representation
of NEMO UBAN motif colored according to the interaction partner,
Ub[distal] (orange) and Ub[proximal] (gold) and both (yellow).
Residues involved in the interaction are labeled.
(E and F)
Open-book representations of the NEMO[CoZi]●diubiquitin
complex. The surfaces of linear diubiquitin (E) and NEMO[CoZi]
(F) are colored according to their electrostatic surface
potential (blue, positive; red, negative). In (F), the bound
diubiquitin is drawn as a transparent ribbon model; Ub[distal]
in orange and Ub[proximal] in gold.
(G and I) Stereo views
of the interactions of the Ub[distal] (G) and Ub[proximal] (I)
with the NEMO UBAN motif colored as in (A). Interacting residues
are shown as sticks. Hydrogen bonds and salt bridges are
indicated as blue dashed lines.
(H and J) Schematic
diagrams of the interactions of Ub[distal] (H) and Ub[proximal]
(J) with the NEMO UBAN motif. The two chains of NEMO are shown
in green and violet, and Ub[distal] and Ub[proximal] in orange
and gold, respectively. Dashed orange and yellow lines indicate
hydrogen bonds and salt bridges, respectively. Hydrophobic
interactions are shown as dashed red lines. Residues in the NEMO
UBAN domain whose mutations are found in ectodermal dysplasia
(D304, E308, and R312) are circled in red.
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