Conformational changes in protein loops and helices induced by post-translational phosphorylation.

ABSTRACT: Post-translational phosphorylation is a ubiquitous mechanism for modulating protein activity and protein-protein interactions. In this work, we examine how phosphorylation can modulate the conformation of a protein by changing the energy landscape. We present a molecular mechanics method in which we phosphorylate proteins in silico and then predict how the conformation of the protein will change in response to phosphorylation. We apply this method to a test set comprised of proteins with both phosphorylated and non-phosphorylated crystal structures, and demonstrate that it is possible to predict localized phosphorylation-induced conformational changes, or the absence of conformational changes, with near-atomic accuracy in most cases. Examples of proteins used for testing our methods includ

SUBMITTER: Groban ES 

PROVIDER: S-EPMC1440919 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature