Figure 4 - full size

 

Figure 4.
Structures of the Ternary Complex, and H3K4me-Binding Cavities (A) Molecular surface representation of hPHD-HD1 binding to H3K4me2 (in yellow cylinder style), with W366 and other critical residues labeled. (B and C) Cylinder representations of (B) semiaromatic K4me2 cavity and (C) A1 cavity, with critical H bonds indicated as dotted lines and hydrophobic contacts as double brackets. (D) Molecular surface representation of PHD, revealing solvent exposure of R2 (regardless of its methylation status). H3K4me, yellow; PHD cavity residues, green. Note that Tern2 has essentially the same structure as Tern1 (shown here; see text). (E) Binding constants of various hPHD point mutants for H3K4me3 15-mer (K[d] values in [mu]M; see also Figure 3 Figure 3-). Mol Cell. 2008 May 23; 30(4-2): 507–518. doi: 10.1016/j.molcel.2008.03.011. Copyright [copyright] 2008 ELL & Excerpta Medica

The above figure is reprinted from an Open Access publication published by Cell Press: Mol Cell (2008, 30, 507-518) copyright 2008.