Figure 2 - full size

 

Figure 2.
Crystal structure of WDR5 bound to MLL1 peptide. A, top and side views of WDR5 bound to MLL1 peptide. The MLL1 peptide is bound to a pocket located at the center of WD40 β-propeller structure, previously shown to be a histone H3-binding pocket. B, F[o]-F[c] map (shown in 3σ) between a refined free WDR5 and data collected from the WDR5-MLLpeptide complex. C, superimposition between WDR5-MLL peptide (blue-green) and WDR5-H3 (yellow-red) complex structures. D, the electrostatic surface potential representations of WDR5-MLL1pep and WDR5-H3K4me2 complex structures. MLL1 peptide and H3K4me2 peptide utilize distinct pockets for binding.

The above figure is reprinted from an Open Access publication published by the ASBMB: J Biol Chem (2008, 283, 35258-35264) copyright 2008.