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Switching on BTK-One Domain at a Time.
Structure 2017 October 4
BTK kinase activity is controlled by multiple inhibitory domains, whose coordinated mechanism of action is poorly understood. In this issue of Structure,Joseph et al. (2017) use solution-based approaches to characterize conformational changes associated with the binding of each inhibitory tether, revealing a multi-step activation process and a previously unknown C-terminal autoinhibitory latch.
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