Disrupting enzyme fluidity

Abstract

A combination of X-ray crystallography, NMR, and mass spectrometry has revealed how diverse small-molecule inhibitors bind Bruton's tyrosine kinase and alter the conformation of this enzyme.

Keywords: allostery; bruton tyrosine kinase; drug resistance; hydrogen/deuterium exchange mass spectrometry; kinase inhibitor; molecular biophysics; none; nuclear magnetic resonance; structural biology.