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Fig. 1 | Journal of Hematology & Oncology

Fig. 1

From: Past, present, and future of Bcr-Abl inhibitors: from chemical development to clinical efficacy

Fig. 1

Structural 3D model of Bcr-Abl catalytic domain. The ribbon diagram of crystal structure shows the N-lobe at the top (dark gray) and C-lobe at the bottom (green), rich in β-sheets and α-helices respectively. The catalytic segment (yellow), the P-loop (red), the activation loop (orange), and the hinge region (light blue) stand in the middle. Key amino acidic residues are indicated in magenta circles: Thr315 (T315) is the gatekeeper residue within the ATP-binding pocket (black arrow), Asp363 (D363) is pivotal for nucleophilic attack on peptide substrate during catalysis, Tyr393 (Y393) is the target of phosphorylation that controls Abl activation and inactivation, whereas the DFG (Asp-Phe-Gly) motif coordinates fundamental cofactors for catalysis, namely Mg2+ ions [88]

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