Mapping allostery through the covariance analysis of NMR chemical shifts.

ABSTRACT: Allostery is a fundamental mechanism of regulation in biology. The residues at the end points of long-range allosteric perturbations are commonly identified by the comparative analyses of structures and dynamics in apo and effector-bound states. However, the networks of interactions mediating the propagation of allosteric signals between the end points often remain elusive. Here we show that the covariance analysis of NMR chemical shift changes caused by a set of covalently modified analogs of the allosteric effector (i.e., agonists and antagonists) reveals extended networks of coupled residues. Unexpectedly, such networks reach not only sites subject to effector-dependent structural variations, but also regions that are controlled by dynamically driven allostery. In these regions the allo

SUBMITTER: Selvaratnam R 

PROVIDER: S-EPMC3076865 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature