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. Author manuscript; available in PMC: 2020 Dec 9.
Published in final edited form as: N Engl J Med. 2019 Dec 12;381(24):2315–2326. doi: 10.1056/NEJMoa1902328

Figure 1. Binding of the Myristoyl Site of the BCR-ABL1 Protein by Asciminib.

Figure 1.

Autoinhibition of the ABL1 kinase occurs through engagement of the myristoyl-binding site by the myristoylated N-terminal — a negative regulatory motif that locks the ABL1 kinase in the inactive state (Panel A). On fusion of ABL1 to BCR, the myristoylated N-terminal is lost and the ABL1 kinase is activated (Panel B). By allosterically binding the myristoyl site, asciminib mimics myristate and restores inhibition of BCR-ABL1 kinase activity (Panel C).