Figure 5.
Fig. 5. Details of the C/EBP protein-DNA
interface. A, hydrophobic cluster involving two thymine moieties
from the C/EBP site and side chains of Val296 and Arg300. B,
interactions defining possible conformation of Arg300. The side
chain of the homologous Arg residue from GCN4 (one observed
conformation) is shown in gray. C, comparison of the protein
environment of base 2 in C/EBP (green) and
GCN4 (gray) complexes. Hydrophobic interaction of the methyl
group from T2 and Ala occurring in GCN4 is marked by a dotted
line. Note that C^2 in the C/EBP site does not interact with
Val296, and its position is displaced relative to T2 from the
GCN4-CREB complex. D, electron density (2F[o] F[c])
contoured at 1.0 (gray) and
1.8 (green;
DNA only) is shown for important residues, with the coordinates
superimposed.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2003,
278,
15178-15184)
copyright 2003.
protein-DNA
interface. A, hydrophobic cluster involving two thymine moieties
from the C/EBP site and side chains of Val296 and Arg300. B,
interactions defining possible conformation of Arg300. The side
chain of the homologous Arg residue from GCN4 (one observed
conformation) is shown in gray. C, comparison of the protein
environment of base 2 in C/EBP 
F[c])
contoured at 1.0 
(gray) and
1.8