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Figure 4.
Figure 4. NMR Structure of the Yng1 PHD Interaction with
Trimethylated H3 K4
NMR-derived structure of the PHD finger
(152–212) in the free form. For clarity, residues 152–154
and 208–212 in the unstructured regions were omitted.
(A)
Backbone superposition of 20 energy-minimized structures of the
PHD finger.
(B) Aromatically rich surface that shows
extensive chemical shift changes upon peptide binding (Y157 and
W180).
(C) Backbone superposition of 20 energy-minimized
structures of the PHD finger in complex with H3[1–9]K4me3
peptide.
(D) Aromatically rich surface that shows extensive
interactions with trimethylated lysine K4 (Y157 and W180).
(E) Surface representation of the YNG1 PHD complex with
H3[1–9]K4me3 peptide. Surface residues that undergo the
largest chemical shift upon binding are highlighted in pink.
(F) An ensemble of 20 structures with side chains involved
in complex formation colored in purple (D172 and E179 for H3 R2,
Y157 and W180 for H3K4).
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