Surface dynamics in allosteric regulation of protein-protein interactions: modulation of calmodulin functions by Ca2+.

ABSTRACT: Knowledge of the structural basis of protein-protein interactions (PPI) is of fundamental importance for understanding the organization and functioning of biological networks and advancing the design of therapeutics which target PPI. Allosteric modulators play an important role in regulating such interactions by binding at site(s) orthogonal to the complex interface and altering the protein's propensity for complex formation. In this work, we apply an approach recently developed by us for analyzing protein surfaces based on steered molecular dynamics simulation (SMD) to the study of the dynamic properties of functionally distinct conformations of a model protein, calmodulin (CaM), whose ability to interact with target proteins is regulated by the presence of the allosteric modulator Ca(2+)

SUBMITTER: Kuttner YY 

PROVIDER: S-EPMC3617199 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature