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Figure 2.
Figure 2. Overall structure of IGF1RK and activation loop
interactions. a, Ribbon diagram of the IGF1RK structure.  -strands
(numbered) are shown in cyan;  -helices
(lettered), in red. The peptide is colored orange with the
phosphate-acceptor Tyr shown in ball-and-stick representation.
The nucleotide analog, AMP-PCP, is also shown in ball-and-stick
representation (black). The dashed gray coil represents the
disordered portion of the kinase insert. The N-terminal (NT) end
of the structure is labeled. The C-terminal end is after J,
hidden behind 8.
b, Interactions within the A-loop (in stereo). The A-loop
(residues 1,123 -1,145) is shown as a backbone worm (green) with
side chains of selected residues shown in stick representation
(carbon = green, nitrogen = blue, oxygen = red, sulfur = yellow
and phosphorus = black). Residues contributing to stabilization
of the activation loop via hydrophobic interactions are shown
with a molecular surface. Hydrogen bonds are shown as dashed
lines (black). c, Interactions between the A-loop and other
kinase segments (in stereo). A backbone worm representation is
shown for the A-loop (green), a segment including part of the
catalytic loop (residues 1,100 -1,105 in orange) and a segment
corresponding to 12
(residues 1,157 -1,159 in gray). Side chain and main chain atoms
are shown in stick representation with the same color scheme as
in (b) with the exception of carbon, which is colored the same
as the corresponding backbone worm. For clarity, pTyr 1136 has
been omitted.
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