Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation.

ABSTRACT: Phospholamban is an integral membrane protein that controls the calcium balance in cardiac muscle cells. As the function and regulation of this protein require the active involvement of low populated states in equilibrium with the native state, it is of great interest to acquire structural information about them. In this work, we calculate the conformations and populations of the ground state and the three main excited states of phospholamban by incorporating nuclear magnetic resonance residual dipolar couplings as replica-averaged structural restraints in molecular dynamics simulations. We then provide a description of the manner in which phosphorylation at Ser16 modulates the activity of the protein by increasing the sizes of the populations of its excited states. These results demonstra

SUBMITTER: De Simone A 

PROVIDER: S-EPMC3844793 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature