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Figure 1.
Structure of the Abl protein.
Type Ia isoform is slightly shorter than type Ib, which contains a
myristoylation (myr) site for attachment to the plasma membrane. Note
the 3 SRC-homology (SH) domains situated toward the NH2
terminus. Y393 is the major site of autophosphorylation within the
kinase domain, and phenylalanine 401 (F401) is highly conserved in PTKs
containing SH3 domains. The middle of each protein is dominated by
proline-rich regions (PxxP) capable of binding to SH3 domains, and it
harbors 1 of 3 nuclear localization signals (NLS). The carboxy terminus
contains DNA as well as G- and F-actin-binding domains.
Phosphorylation sites by Atm, cdc2, and PKC are shown. The arrowhead
indicates the position of the breakpoint in the Bcr-Abl fusion
protein.
