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Figure 4.
Figure 4 Interaction between WDR5 and histone peptides. (A)
H3K4me2 peptide is shown in a stick model colored in yellow, and
residues in WDR5 that make hydrogen bonds with H3K4me2 are also
shown in a stick model and colored in blue. Hydrogen bonds are
denoted as orange dotted lines. (B) Interaction of different
states of H3K4 with Glu322 in WDR5. Dimethylated K4 is shown as
a stick model colored in yellow, which interacts with Glu322 in
WDR5, colored in yellow, via a water molecule. Unmodified K4 in
the WDR5–H3K4 complex is colored in cyan, which is stabilized
by crystal contacts. The side chain of Glu322 in this complex is
either disordered or points to solvent. In the WDR5  23–H3K4me
complex structure, the side chain of K4me is disordered. The
side chain of Glu322 is either disordered or adopts the
conformation of Glu322 in the WDR5 23–H3K4me2
complex. K4me3 in the WDR5–H3K4me3 complex is disordered, and
Glu322, colored in magenta, points to solvent.
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