Coherent conformational degrees of freedom as a structural basis for allosteric communication.

ABSTRACT: Conformational changes in allosteric regulation can to a large extent be described as motion along one or a few coherent degrees of freedom. The states involved are inherent to the protein, in the sense that they are visited by the protein also in the absence of effector ligands. Previously, we developed the measure binding leverage to find sites where ligand binding can shift the conformational equilibrium of a protein. Binding leverage is calculated for a set of motion vectors representing independent conformational degrees of freedom. In this paper, to analyze allosteric communication between binding sites, we introduce the concept of leverage coupling, based on the assumption that only pairs of sites that couple to the same conformational degrees of freedom can be allosterically connec

SUBMITTER: Mitternacht S 

PROVIDER: S-EPMC3234217 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature