Figure 1.
FIGURE 1. Three-dimensional crystal structure of the
complex of ING4-PHD bound to H3[10]K4me3. A, overall structure
with ING4-PHD shown in gray and H3[10]K4me3 shown in yellow
stick representation. The location of the ING4 residues lining
the binding grooves for histone 3 residues Ala^1, Arg^2, Thr^3,
Lys^4, and Ser^10 is indicated with black labels. B, view of a
2(|F[o]| - |F[c]|) omit map at 1.76 Å contoured at 1 as a
blue mesh. The omit map was calculated with the program OMIT in
the CCP4 package (45). C, details of the β-sheet structure
formed by H3 residues Arg^2–Thr^6 and ING4 residues
Gly^207–Gly^211 with backbone hydrogen bonds in green. D,
details of side chain interactions with hydrogen bonds and water
molecules in green.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2008,
283,
15956-15964)
copyright 2008.
as a
blue mesh. The omit map was calculated with the program OMIT in
the CCP4 package (45). C, details of the β-sheet structure
formed by H3 residues Arg^2–Thr^6 and ING4 residues
Gly^207–Gly^211 with backbone hydrogen bonds in green. D,
details of side chain interactions with hydrogen bonds and water
molecules in green.