Dynamic equilibria in protein kinases

Structural changes involved in protein kinase activation and ligand binding have been determined from a wealth of X-ray crystallographic evidence. Recent solution studies using NMR, EPR, HX-MS, and fluorescence techniques have deepened this understanding by highlighting the underlying energetics and dynamics of multistate conformational ensembles. This new research is showing how activation mechanisms and ligand binding alter the internal motions of kinases and enable allosteric coupling between distal regulatory regions and the active site.

Automated summary

Recent research utilizing various techniques has unveiled the structural changes involved in protein kinase activation and ligand binding, deepening our understanding of these processes. This research demonstrates how activation mechanisms and ligand binding affect the internal motions of kinases, enabling allosteric coupling between distal regulatory regions and the active site.