Elastic network model of allosteric regulation in protein kinase PDK1.

ABSTRACT:

Background

Structural switches upon binding of phosphorylated moieties underpin many signalling networks. The ligand activation is a form of allosteric modulation of the protein, where the binding site is remote from the structural change in the protein. Recently this structural switch has been elegantly demonstrated with the crystallisation of the activated form of 3-phosphoinositide-dependent protein kinase-1 (PDK1). The purpose of the present work is to determine whether the allosteric coupling in PDK1 emerges at the level of a simple coarse grained model of protein dynamics.

Results

It is shown here that the allosteric effects of the agonist binding to the small lobe upon the activation loop in the large lobe of PDK1 are explainable within a simple 'ball and spring' elas

SUBMITTER: Williams G 

PROVIDER: S-EPMC2888814 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature