Figure 3.
Figure 3. IGF1RK peptide substrate binding and comparison to
IRK. a, Stereo view of the 2F[o] - F[c] electron density map
(2.1 Å resolution, 1 contour)
for the peptide substrate. The electron density is shown as a
wire mesh (blue); the peptide substrate (orange), in stick
representation. b, Stereo view of interactions at the IGF1RK
-peptide substrate interface. A semitransparent molecular
surface (gray) of IGF1RK is shown with residues (labeled and
displayed in stick representation) that define the peptide
binding cleft and interact with the peptide substrate. The
peptide (shown in stick representation) is illustrated without a
molecular surface, with residues labeled relative to the
phosphate acceptor Tyr (P0). Hydrogen bonds between the peptide
and the enzyme are shown as black lines. Bond coloring is carbon
= orange, oxygen = red, nitrogen = blue, sulfur = green and
phosphorus = yellow. c, A molecular surface representation of
IGF1RK illustrating surface residue differences between IGF1RK
and IRK. The molecular surface contributed by differing side
chains between the two structures are colored green. The
molecular surface contributed by the Thr 1053 side chain in the
interlobe linker is colored yellow (see text). d, A backbone
worm representation of IGF1RK. Segments corresponding to
residues that differ between IGF1RK and IRK are colored green.
In (c,d), stick representations of the nucleotide analog
(AMP-PCP) and peptide are shown. The semitransparent segment
represents the portion of the kinase insert disordered in the
structure. Bond coloring is the same as in (a).
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2001,
8,
1058-1063)
copyright 2001.
contour)
for the peptide substrate. The electron density is shown as a
wire mesh (blue); the peptide substrate (orange), in stick
representation. b, Stereo view of interactions at the IGF1RK
-peptide substrate interface. A semitransparent molecular
surface (gray) of IGF1RK is shown with residues (labeled and
displayed in stick representation) that define the peptide
binding cleft and interact with the peptide substrate. The
peptide (shown in stick representation) is illustrated without a
molecular surface, with residues labeled relative to the
phosphate acceptor Tyr (P0). Hydrogen bonds between the peptide
and the enzyme are shown as black lines. Bond coloring is carbon
= orange, oxygen = red, nitrogen = blue, sulfur = green and
phosphorus = yellow. c, A molecular surface representation of
IGF1RK illustrating surface residue differences between IGF1RK
and IRK. The molecular surface contributed by differing side
chains between the two structures are colored green. The
molecular surface contributed by the Thr 1053 side chain in the
interlobe linker is colored yellow (see text). d, A backbone
worm representation of IGF1RK. Segments corresponding to
residues that differ between IGF1RK and IRK are colored green.
In (c,d), stick representations of the nucleotide analog
(AMP-PCP) and peptide are shown. The semitransparent segment
represents the portion of the kinase insert disordered in the
structure. Bond coloring is the same as in (a).