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. 2010 Jul 12;49(31):6576–6586. doi: 10.1021/bi1009387

Figure 4.

Figure 4

Identification of the H3K4me3 recognition site on PHD3. (A) Superimposition of the MLL PHD3 finger with the BPTF PHD finger in complex with H3K4me3 (PDB entry 2F6J). The MLL PHD3 finger is colored blue, the BPTF PHD finger green, and the N-terminal H3 tail red. The side chain of the consensus tryptophan of each PHD finger is colored yellow. The side chain of the K4 of histone H3 is colored blue. (B) Surface comparison of the MLL PHD3 finger (right) with the BPTF PHD finger in complex with H3K4me3 (left). The N-terminal H3 tail is colored red, and the side chains of R2 and K4 are colored blue. Residues whose backbone resonance was broadened out (yellow) or significantly perturbed (red) in panel C are mapped on the structure of the MLL PHD3 finger. (C) Plot of chemical shift differences (Δδtot) of the backbone HN and N resonances of PHD3 between the free and H3K4me3-bound state. Asterisks indicate the residues whose resonances are broadened out. (D) Overlay of 15N−1H HSQC spectra of the W1594A mutant in the presence (blue) and absence (red) of H3K4me3.