Figure 2.
Figure 2: Crystal structures of human BPTF PHD
finger-linker-bromodomain in the free state and bound to
H3(1–15)K4me3. a, Domain architecture of BPTF bromodomain
and proximal PHD finger. b, Ribbon representation of the crystal
structure of the BPTF PHD finger-linker-bromodomain in the free
state. Two bound Zn ions within the PHD fold are shown as balls.
c, Crystal structure of the H3(1–15)K4me3-bound complex, with
bound peptide shown in a space-filling representation. d,
Structure of the PHD finger complex with the 2F[o] - F[c] omit
electron density (0.8 level)
highlighted for the bound H3(1–15)K4me3 peptide. e,
Positioning of the H3(1–15)K4me3 peptide (space-filling
representation) on the surface of the PHD finger portion
(electrostatic surface representation with red as negatively
charged and blue as positively charged surface) of the complex.
f, Different view emphasizing the positioning of R2 and K4me3 in
adjacent channels.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2006,
442,
91-95)
copyright 2006.
level)
highlighted for the bound H3(1–15)K4me3 peptide. e,
Positioning of the H3(1–15)K4me3 peptide (space-filling
representation) on the surface of the PHD finger portion
(electrostatic surface representation with red as negatively
charged and blue as positively charged surface) of the complex.
f, Different view emphasizing the positioning of R2 and K4me3 in
adjacent channels.