Format

Send to

Choose Destination
Structure. 2017 Oct 3;25(10):1469-1470. doi: 10.1016/j.str.2017.09.012. Epub 2017 Oct 3.

Switching on BTK-One Domain at a Time.

Author information

1
Cardiovascular Research Institute, University of California, San Francisco, San Francisco, CA 94158, USA.
2
Cardiovascular Research Institute, University of California, San Francisco, San Francisco, CA 94158, USA; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: natalia.jura@ucsf.edu.

Abstract

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.

PMID:
28978404
DOI:
10.1016/j.str.2017.09.012
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center