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Figure 2.
Figure 2. NMR Structure of the PCAF Bromodomain/Tat AcK50
Peptide Complex(A) Stereoview of the backbone atoms (N, Cα, and
C′) of 25 superimposed NMR-derived structures of the PCAF
bromodomain (black) (showing residues 719–830) in complex with
the Tat AcK50 peptide (green) (showing residues 46–55). Note
that amino acid residues in the Tat peptide are described either
according to their relative positions with respect to the
acetyl-lysine in the sequence or for clarity numbered by their
specific positions in the protein sequence of Tat.(B) Ribbons
(Carson, 1991) representation of the average minimized NMR
structure of the PCAF bromodomain/Tat peptide complex.(C)
Stereoview of the Tat binding site in the bromodomain showing
side chains of the protein (green) and peptide (blue) residues
that are directly involved intermolecular interactions.(D)
Stereoview of superimposition of the free (green) and
ligand-bound (blue) structures of PCAF bromodomain showing side
chain conformation of the residues in the Tat peptide binding
site. The residues of the Tat peptide are colored in orange.(E)
Surface representation of the Tat binding site of the
bromodomain in ligand-bound (left) and free form (right).
Protein residues important in ligand recognition are colored
with the same color scheme in both structures. Residues
indicated by an asterisk are almost completely buried in the
free form structure.
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