Automated identification of binding sites for phosphorylated ligands in protein structures.

ABSTRACT: Phosphorylation is a crucial step in many cellular processes, ranging from metabolic reactions involved in energy transformation to signaling cascades. In many instances, protein domains specifically recognize the phosphogroup. Knowledge of the binding site provides insights into the interaction, and it can also be exploited for therapeutic purposes. Previous studies have shown that proteins interacting with phosphogroups are highly heterogeneous, and no single property can be used to reliably identify the binding site. Here we present an energy-based computational procedure that exploits the protein three-dimensional structure to identify binding sites involved in the recognition of phosphogroups. The procedure is validated on three datasets containing more than 200 proteins binding to AT

SUBMITTER: Ghersi D 

PROVIDER: S-EPMC4266509 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature