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Figure 1.
Figure 1. Structure of the Taz2-p53[2–39] Complex
(A)
Stereo image of the overlay of ten lowest-energy NMR structures
of the complex between p53[15–27] (magenta) and the Taz2
domain of p300 (gray). The structures are superimposed on the
Cα traces.
(B) Plot of backbone amide ^15N-{^1H}
heteronuclear NOEs of p53[2–39].
(C) Cylinder model of
the average conformation of the complex. p53 is shown in magenta
and the helices of Taz2 are shown in blue (α1), lilac (α2),
orange (α3), and red (α4). Zinc ions in Taz2, modeled as green
spheres, were added according to zinc-coordination distances
into the known binding cage.
(D) Secondary chemical shift
difference of p53[2-39] in the complex (measured Cα chemical
shift − random coil value).
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