NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles.

ABSTRACT: Phospholamban is an integral membrane protein that regulates the contractility of cardiac muscle by maintaining cardiomyocyte calcium homeostasis. Abnormalities in association of protein kinase A with PLB have recently been linked to human heart failure, where a single mutation is responsible for dilated cardiomyopathy. To date, a high-resolution structure of phospholamban in a lipid environment has been elusive. Here, we describe the first structure of recombinant, monomeric, biologically active phospholamban in lipid-mimicking dodecylphosphocholine micelles as determined by multidimensional NMR experiments. The overall structure of phospholamban is "L-shaped" with the hydrophobic domain approximately perpendicular to the cytoplasmic portion. This is in agreement with our previously publi

SUBMITTER: Zamoon J 

PROVIDER: S-EPMC1303482 | biostudies-literature | 2003 Oct

REPOSITORIES: biostudies-literature