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Figure 1.
Fig. 1. Crystal structure of the catalytic domain of Abelson
tyrosine kinase complexed with a variant of STI-571. (A)
Structural formula of the Abl inhibitor STI-571 (panel 1) and
the variant (panel 2) used in this crystallographic study. (B)
Ribbon representation of the three-dimensional structure of Abl
kinase domain in complex with the STI-571 variant shown in (A).
The molecular surface of the inhibitor is shown. A central
conserved region of the kinase, the catalytic segment, is shown
in green and the activation loop in magenta. (C) Ribbon
representation of the activation loop of Abl. The polypeptide
backbone of the activation loop is shown in magenta.
Hydrogen-bonding interaction are depicted by dashed lines.
Tyr393 is the site of phosphorylation within the activation
loop. (D) The polypeptide region in the vicinity of the Tyr393
is shown. Superimposed is the peptide substrate (green), as seen
in the structure of insulin receptor tyrosine kinase (IRK)
complexed with peptide substrate (14), and the activation loop
of IRK in the inactive form (light pink) (32). The figure was
generated by superimposing the catalytic segments of the two
kinases.
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