Figure 2.
Figure 2. Recognition of the histone H3 N terminus by WDR5.
(a) Stereo view of the simulated annealing F[o] - F[c] omit map
(green). Electron density is contoured at 2.0 .
Gray carbons, WDR5; yellow carbons, histone H3. Q5 in histone H3
was omitted from the image for clarity. (b) Schematic
representation of the interactions observed between WDR5 and
histone H3. Residues in the protein that engage in van der Waals
contacts, hydrogen bonds or salt bridge interactions with
histone H3 are shown. Hydrogen bonds and salt bridge
interactions are delineated by orange dashed lines. (c)
Superimposition of the histone H3–binding cleft of apo-WDR5
(green) and the WDR5–histone H3 complex (blue), showing
structural rearrangements that occur upon histone binding.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2006,
13,
698-703)
copyright 2006.
.
Gray carbons, WDR5; yellow carbons, histone H3. Q5 in histone H3
was omitted from the image for clarity. (b) Schematic
representation of the interactions observed between WDR5 and
histone H3. Residues in the protein that engage in van der Waals
contacts, hydrogen bonds or salt bridge interactions with
histone H3 are shown. Hydrogen bonds and salt bridge
interactions are delineated by orange dashed lines. (c)
Superimposition of the histone H3–binding cleft of apo-WDR5
(green) and the WDR5–histone H3 complex (blue), showing
structural rearrangements that occur upon histone binding.