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Figure 3.
Figure 3: Conserved interactions in the ACTR -CBP complex. a,
Sequence alignment of the CBP binding domain of human ACTR(1018
-1088) and a representative set of p160 coactivators. b,
Sequence alignment of the ACTR binding domain of murine CBP with
other members of the CBP/p300 family. Conserved hydrophobic
residues (green), conserved acidic residues (red), conserved
basic residues (blue), and other conserved residues (orange) are
indicated (h, human; m, murine, x, Xenopus laevis; d,
Drosophila; dr, Danio rerio; c, Caenorhabditis elegans). c,  -X-X-
-
and
-
-X-X-
hydrophobic
contact map defining the interface between ACTR and CBP ( denotes
hydrophobic residue). The four -X-X-
-
motifs
that comprise the hydrophobic core are enclosed by a green box.
The buried intermolecular salt bridge is indicated. d, Close-up
of the salt bridge between Arg 2105 and Asp 1068 salt bridge.
The solvent-accessible surface of ACTR is shown.
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