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Figure 3.
Figure 3. Structural Differences between c-Myb R2 and AMV
v-Myb R2 and Close-Up Views of the Interactions among c-Myb,
C/EBPβ, and DNA(A) Stereo view of the superimposed R2 domains
within c-Myb (pink) and AMV v-Myb (gray) complexes. The peptide
backbones are drawn as tubes, and the side chains of residues
that are mutated or exhibit different conformations in AMV v-Myb
are drawn as sticks.(B) A close-up view of the interactions
between the Arg114 and Trp115 backbones and the DNA phosphate
oxygens at G4′ within the c-Myb and AMV v-Myb complexes.(C)
Stereo view of the c-Myb–C/EBPβ interaction site.
Intermolecular hydrogen bonds and K^+-mediated interactions are
represented by dotted lines. Parts of c-Myb and C/EBPβ chains A
and B are drawn as pink, yellow, and green sticks, respectively.
The part of the DNA backbone interacting with the C/EBPβ
leucine zipper region is also shown. The metal binding sites of
R1, R2, and R3 were confirmed by their high-resolution crystal
structures (T.T. et al., submitted).(D) Summary of the
intermolecular van der Waals interactions between c-Myb and
C/EBPβ.(E) Stereo view of the c-Myb–C/EBPβ-DNA interaction
site highlighting the interactions involved in stabilization of
the α1–α2 loop of c-Myb R2. The peptide backbones of
DNA-bound c-Myb (pink) and C/EBPβ chains A (yellow) and B
(green) are drawn as tubes. Free c-Myb R2 (blue) is superimposed
on the DNA-bound c-Myb R2. An alternative position for the
disordered portion of the α1–α2 loop of the free c-Myb R2 is
colored dark blue.
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