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Significance Bruton’s tyrosine kinase (BTK) is targeted in treatment of immune cancers. As patients experience drug resistance, there is a need for alternative approaches to inhibit BTK. Other recently published findings clarify the role of the BTK pleckstrin homology (PH) domain in mediating activation via dimerization and sensing of ligand concentration at the membrane. Work presented here provides insight into the autoinhibitory BTK structure that has so far been elusive via crystallographic methods. In the resting state, the BTK PH domain binds to the activation loop face of the kinase domain and allosterically alters key sites within the kinase domain. The findings define a new regulatory site, the PH/kinase interface, that can be exploited in drug discovery efforts.

Lipid-targeting pleckstrin homology domain turns its autoinhibitory face toward the TEC kinases