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Figure 2.
(a) Residues 1–7 of the H3 peptide (yellow tube) interact
with the active site cavity of LSD1. Molecular surface of LSD1
AOD and SWIRM is colored by electrostatic potential: red,
negative; blue, positive. Dashed yellow line represents
C-terminal portion of H3, which might bind at a surface groove
between AOD and SWIRM, according to existing biochemical
evidence^8, ^9. (b) Binding of H3 at the active site of LSD1.
Yellow, H3; purple, LSD1. (c) Binding of an H3K4me3 peptide to
the PHD finger of BPTF (PDB 2FUU). Color scheme is as in b. (d)
Stereo view of an H3K4me3 peptide bound to the PHD finger of
ING2 (PDB 2G6Q). The distance between the C  atoms
of Arg2 and Thr6 is 13.1 Å. (e) Stereo view of the
derivatized H3 peptide bound to LSD1 (same scale as e). Dashed
red lines represent the hydrogen bonds of the three  -turns.
The distance between the C atoms
of Arg2 and Thr6 is 9.2 Å. (f) Schematic drawing of
interactions between LSD1 and the H3 peptide, highlighting the
anionic pocket and the serpentine H3 backbone conformation that
results from the three -turns.
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