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The Dawn of Allosteric BCR-ABL1 Drugs: From a Phenotypic Screening Hit to an Approved Drug
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    The Dawn of Allosteric BCR-ABL1 Drugs: From a Phenotypic Screening Hit to an Approved Drug
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    Journal of Medicinal Chemistry

    Cite this: J. Med. Chem. 2022, 65, 11, 7581–7594
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    https://doi.org/10.1021/acs.jmedchem.2c00373
    Published May 24, 2022
    Copyright © 2022 American Chemical Society

    Abstract

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    Chronic myeloid leukemia (CML) is driven by the constitutive activity of the BCR-ABL1 fusion oncoprotein. Despite the great success of drugs that target the BCR-ABL1 ATP-binding site in transforming CML into a manageable disease, emerging resistance point mutations impair inhibitor binding, thereby limiting the effectiveness of these drugs. Recently, allosteric inhibitors that interact with the ABL1 myristate-binding site have been shown to awaken an endogenous regulatory mechanism and reset full-length BCR-ABL1 into an inactive assembled state. The discovery and development of these allosteric inhibitors demonstrates an in-depth understanding of the fundamental regulatory mechanisms of kinases. In this review, we illustrate the structural basis of c-ABL1’s dynamic regulation of autoinhibition and activation, discuss the discovery of allosteric inhibitors and the characterization of their mechanism of action, present the therapeutic potential of dual binding to delay the development of mutation-driven acquired resistance, and suggest key lessons learned from this program.

    Copyright © 2022 American Chemical Society

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    Cited By

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    This article is cited by 7 publications.

    1. Mingzhen Zhang, Yonglan Liu, Hyunbum Jang, Ruth Nussinov. Strategy toward Kinase-Selective Drug Discovery. Journal of Chemical Theory and Computation 2023, 19 (5) , 1615-1628. https://doi.org/10.1021/acs.jctc.2c01171
    2. Mingxing Teng, Damian W. Young, Zhi Tan. The Pursuit of Enzyme Activation: A Snapshot of the Gold Rush. Journal of Medicinal Chemistry 2022, 65 (21) , 14289-14304. https://doi.org/10.1021/acs.jmedchem.2c01291
    3. Maria-Jesus Blanco, Kevin M. Gardinier, Mark N. Namchuk. Advancing New Chemical Modalities into Clinical Studies. ACS Medicinal Chemistry Letters 2022, 13 (11) , 1691-1698. https://doi.org/10.1021/acsmedchemlett.2c00375
    4. Bengi Ruken Yavuz, Chung-Jung Tsai, Ruth Nussinov, Nurcan Tuncbag. Pan-cancer clinical impact of latent drivers from double mutations. Communications Biology 2023, 6 (1) https://doi.org/10.1038/s42003-023-04519-5
    5. Ruth Nussinov, Mingzhen Zhang, Yonglan Liu, Hyunbum Jang. AlphaFold, allosteric, and orthosteric drug discovery: Ways forward. Drug Discovery Today 2023, 28 (6) , 103551. https://doi.org/10.1016/j.drudis.2023.103551
    6. Yang-Yang Gao, Wei-Cheng Yang, Charles R. Ashby, Ge-Fei Hao. Mapping cryptic binding sites of drug targets to overcome drug resistance. Drug Resistance Updates 2023, 67 , 100934. https://doi.org/10.1016/j.drup.2023.100934
    7. Yonglan Liu, Mingzhen Zhang, Chung-Jung Tsai, Hyunbum Jang, Ruth Nussinov. Allosteric regulation of autoinhibition and activation of c-Abl. Computational and Structural Biotechnology Journal 2022, 20 , 4257-4270. https://doi.org/10.1016/j.csbj.2022.08.014

    Journal of Medicinal Chemistry

    Cite this: J. Med. Chem. 2022, 65, 11, 7581–7594
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.jmedchem.2c00373
    Published May 24, 2022
    Copyright © 2022 American Chemical Society

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