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. 2024 Apr 8;12:RP92324. doi: 10.7554/eLife.92324

Figure 1. Domain organization of Abl and ligand-induced conformations of the Abl core.

Figure 1.

(A) Domain organization of Abl isoforms 1a,b and of the chronic myeloid leukemia (CML)-inducing fusion protein Bcr-Abl. (B) Crystal structure of the N-terminally myristoylated Abl 1b isoform (residues 2–531, PDB 2FO0). SH3 domain (green), SH2 domain (yellow), KD-SH2 linker (grey), kinase domain (KD) N- and C-lobes (KD-N and KD-C, respectively, blue), activation loop (A-loop, green), and αI-helix (cyan) are shown in cartoon representation. The myristoyl is shown as yellow spheres. The N-cap (aa 2–82), which is largely not observed in the crystal, is indicated as a dashed brown line. A schematic representation on the right indicates the position of the kink in the αI-αI’ helix. (C) Alignment of the crystal structure of a KD-only construct with unliganded myristoyl pocket (blue, PDB 1M52) with the assembled Abl core structure (PDB 2FO0). The SH3 and SH2 domains of the latter are displayed as in panel B. (D) Model of a single conformation of the dynamical imatinib-bound, disassembled Abl core as derived by NMR and SAXS (Skora et al., 2013). The coloring follows panel B with the exception of the activation loop (magenta). Imatinib is shown as magenta sticks. Blue arrows indicate relative motions of the SH3, SH2, and KD domains.