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It was recently established that binding of type II ATP site inhibitors, such as imatinib, generates a force from the KD N-lobe onto the SH3 domain and in consequence disassembles the core. Here, we demonstrate that the C-terminal \u03b1I-helix exerts an additional force toward the SH2 domain, which correlates both with kinase activity and type II inhibitor-induced disassembly. The \u03b1I-helix mutation E528K, which is responsible for the ABL1 malformation syndrome, strongly activates Abl by breaking a salt bridge with the KD C-lobe and thereby increasing the force onto the SH2 domain. In contrast, the allosteric inhibitor asciminib strongly reduces Abl\u2019s activity by fixating the \u03b1I-helix and reducing the force onto the SH2 domain. These observations are explained by a simple mechanical model of Abl activation involving forces from the KD N-lobe and the \u03b1I-helix onto the KD\/SH2SH3 interface.<\/jats:p>","DOI":"10.7554\/elife.92324","type":"journal-article","created":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T13:52:10Z","timestamp":1698846730000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.92324","source":"Crossref","is-referenced-by-count":5,"title":["The molecular basis of Abelson kinase regulation by its \u03b1I-helix"],"prefix":"10.7554","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7920-2219","authenticated-orcid":true,"given":"Johannes","family":"Paladini","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02s6k3f65","id-type":"ROR","asserted-by":"publisher"}],"name":"Structural Biology and Biophysics, Biozentrum, University of Basel","place":["Basel, 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