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. Author manuscript; available in PMC: 2016 Jan 4.
Published in final edited form as: Nat Struct Mol Biol. 2006 Jul 9;13(8):704–712. doi: 10.1038/nsmb1119

Figure 1.

Figure 1

The overall structure of WDR5 complexes with histone H3. (a) The set of possible methylation states of H3K4. In general, nucleosomes di- and trimethylated at K4 of H3 are associated with transcriptional activation. (b) The overall structure of WDR5 in complex with H3K4me2. WDR5 is a canonical seven-bladed β-propeller (red); the histone H3 peptide binds across the top face of the protein (green, with amino (N′) and carboxyl (C′) termini and R2 labeled). (c) Electrostatic surface of WDR5 contoured from −8 to +8 kT using ABPS52 shows a series of acidic patches on the upper face of WDR5 (arrows 1–4), whereas the remainder of the protein is highly positively charged. H3K4me2 peptide is shown in green; potential aromatic cage residues are situated around arrow 5. Remaining arrows indicate patches of positive electrostatic potential discussed in the text. Cutaway view of this surface along the pseudo seven-fold symmetry axis (top) demonstrates how deeply buried R2 is in the cavity of the β-propeller fold's torus.