Molecular mechanisms of BCR::ABL1 in chronic myeloid leukaemia: From treatment-free remission to curative therapy

Figure 1 Different conformations of the ABL1 kinase domain. A: The active conformation of the ABL1 kinase domain showing the activation loop (A-loop) which is open, the phosphate-binding loop (P-loop) and the αC helix; B: The inactive conformation of the ABL1 kinase domain when bound to TKI showing the A-loop closed; C: The autoinhibited conformation of the ABL1 kinase domain showing the engagement of the N-terminal myristoyl group within the myristoylation pocket, clamped by the SH2 and SH3 domains. Citation: Wu A, Liu X, Fruhstorfer C, Jiang X. Clinical Insights into Structure, Regulation, and Targeting of ABL Kinases in Human Leukemia. Int J Mol Sci 2024; 25: 3307 [PMID: 38542279 DOI: 10.3390/ijms25063307].