Mapping Allostery through Equilibrium Perturbation NMR Spectroscopy

摘要

Allostery is a fundamental mechanism for regulating biological function through ligand binding.While understanding the structural basis of allosteric control relies on the comparative analysis of macromolecules in their free and bound states,the direct free versus bound comparison is often experimentally challenging due to the instability of one of the two forms.This is the case for the regulatory subunit(R)of the prototypical and ubiquitous protein kinase A(PKA),which is the main eukaryotic receptor for the cAMP second messenger.