1. Switching on BTK—One Domain at a Time
Christopher Agnew, Natalia Jura 
Structure 
Volume 25, Issue 10, Pages (October 2017)
DOI: /j.str
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2. Figure 1
Regulation of Non-receptor Tyrosine Kinases through multi-domain Inhibitory Tethers
(A) Schematic representation of conformational transitions occurring in full-length BTK on its pathway to full kinase activation that incorporates insights provided by Joseph et al., 2017 in this issue of Structure. In this model, in the fully inhibited state, SH3 and SH2 domains bind to the back of the kinase domain, while the PHTH domain binds in the vicinity of the active site. The PRR segment remains disengaged from the SH3 domain. Binding of the PRR segment to the SH3 domain and/or release of the electrostatic latch is expected to push the equilibrium toward an active conformation, which is fully established by lipid binding to the PHTH domain, which by promoting “Saraste dimer” increases kinase autophosphorylation leading to full BTK kinase activity.
(B) Schematic representation of the modular architecture of the SRC, ABL, and TEC family kinases depicting the C-terminal autoinhibitory latch.
Structure  , DOI: ( /j.str )
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