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Figure 3.
Figure 3. Structural comparisons. (A) Xenopus and Drosophila
SANT domains are colored in green and grey, respectively. The
additional N-terminal helix in the Drosophila protein is in red,
and the C-terminal SLIDE domain is shaded in yellow. The
proteolytic cleavage site in the Xenopus protein is indicated.
(B) Xenopus SANT domain and cMyb R2R3 are colored in green and
magenta, respectively (middle panel). Structural alignment of
helices  D,
E,
and F
of Xenopus SANT and that of R2 of c-Myb R2R3 (PDB 1GV2) derived
the superimposition. The left panel shows the acidic surface
patch of Xenopus SANT and the right panel shows the
corresponding region of basic DNA binding surface of R2 of c-Myb
R2R3. (C) X-ray structure of c-Myb R2R3[11] with the locations
of three hydrophobic residues whose mutation to polar or charged
side chains affecting the ability of v-Myb interaction with
histone (left panel). A surface groove on the opposite side of
the DNA binding might be the binding groove for histone H3
peptide.
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