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Figure 5.
Figure 5. Acidic surface of IRF-3. (a) The electrostatic
surface potential representation of the IRF-3 homodimer. The
surface corresponds to the opposite surface shown in Figure 2a.
Figure 5a was prepared with GRASP36 and Raster3D^34. (b) Dimer
formation of the E/A mutant. Expression vectors for p50-tagged
wild type and the E/A mutant of IRF-3 were transiently expressed
in L929 cells. After mock treatment (-) or infection with NDV
for 12 h (+), the extracts were prepared and subjected to native
PAGE using anti-p50-tag as a probe. (c) Critical role of
glutamate residues in the association of p50-tagged IRF-3 with
p300/CBP. The extracts in Figure 5c were immunoprecipitated with
anti-NES, and resolved by SDS-PAGE followed by immunoblotting
with anti-p300/CBP (top) or anti-p50-tag (bottom).
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