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Figure 3.
Figure 3. Abl-AMN107 complex
A: Superposition of AMN107
(magenta) bound to Abl^M351T (orange), and imatinib (green)
bound to Abl (yellow). H bonds within the AMN107-Abl^M351T
complex are depicted as dashed red lines, whereas those in the
imatinib complex are shown in black. The variability in the
positions of side chains from the C-helix (top right corner) is
due to crystal contacts that influence the position of the
N-terminal lobe of the kinase. The methyl-imidazole group of
AMN107 packs in a hydrophobic pocket formed by these residues
with the nitrogen exposed to solvent.
B: Superposition of
parts of the backbone structures of imatinib-Abl (yellow),
AMN107-Abl^M351T (orange), and AMN107-Abl (cyan). The inhibitors
are shown in green, magenta and blue, respectively. The small
black arrows show the shifts within helix E and the preceding
loop, DE. Figure 3. Abl-AMN107 complexA: Superposition of
AMN107 (magenta) bound to Abl^M351T (orange), and imatinib
(green) bound to Abl (yellow). H bonds within the
AMN107-Abl^M351T complex are depicted as dashed red lines,
whereas those in the imatinib complex are shown in black. The
variability in the positions of side chains from the C-helix
(top right corner) is due to crystal contacts that influence the
position of the N-terminal lobe of the kinase. The
methyl-imidazole group of AMN107 packs in a hydrophobic pocket
formed by these residues with the nitrogen exposed to solvent.B:
Superposition of parts of the backbone structures of
imatinib-Abl (yellow), AMN107-Abl^M351T (orange), and AMN107-Abl
(cyan). The inhibitors are shown in green, magenta and blue,
respectively. The small black arrows show the shifts within
helix E and the preceding loop, DE.
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