Figure 3.
FIGURE 3. Comparison of the structures of H3K4me3 peptides
bound to ING4 and ING2 PHD. A, the crystal structure of ING4-PHD
is shown as a gray surface with the bound H3[10]K4me3 in yellow
and the superimposed H3[12]K4me3 from the corresponding ING2-PHD
complex structure in green. Only H3 residues Ala^1 to Arg^8 are
seen in the crystal of the ING2 complex (Protein Data Bank entry
2G6Q). Black labels indicate the C atoms of the peptide
residues, whose positions are very similar in both peptides up
to H3 Thr^6. B, surface representations of the PHD fingers of
ING2 and ING4 bound to the histone peptides where the
electrostatic potential is indicated by a gradient of red
(negative charge) and blue (positive charge) colors. The
positions of the homologous tyrosine residues 198 and 215 are
indicated in ING4 and ING2, respectively.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2008,
283,
15956-15964)
copyright 2008.
atoms of the peptide
residues, whose positions are very similar in both peptides up
to H3 Thr^6. B, surface representations of the PHD fingers of
ING2 and ING4 bound to the histone peptides where the
electrostatic potential is indicated by a gradient of red
(negative charge) and blue (positive charge) colors. The
positions of the homologous tyrosine residues 198 and 215 are
indicated in ING4 and ING2, respectively.