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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Traaseth, Nathaniel J. Torgersen, Kurt D. Karim, Christine B. Veglia, Gianluigi Thomas, David D. Verardi, Raffaello |
| Description | Author Affiliation: Traaseth NJ ( Department of Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.); |
| Abstract | Phospholamban (PLN) regulates calcium translocation within cardiac myocytes by shifting sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) affinity for calcium. Although the monomeric form of PLN (6 kDa) is the principal inhibitory species, recent evidence suggests that the PLN pentamer (30 kDa) also is able to bind SERCA. To date, several membrane architectures of the pentamer have been proposed, with different topological orientations for the cytoplasmic domain: (i) extended from the bilayer normal by 50-60 degrees; (ii) continuous alpha-helix tilted 28 degrees relative to the bilayer normal; (iii) pinwheel geometry, with the cytoplasmic helix perpendicular to the bilayer normal and in contact with the surface of the bilayer; and (iv) bellflower structure, in which the cytoplasmic domain helix makes approximately 20 degrees angle with respect to the membrane bilayer normal. Using a variety of cell membrane mimicking systems (i.e., lipid vesicles, oriented lipid bilayers, and detergent micelles) and a combination of multidimensional solution/solid-state NMR and EPR spectroscopies, we tested the different structural models. We conclude that the pinwheel topology is the predominant conformation of pentameric PLN, with the cytoplasmic domain interacting with the membrane surface. We propose that the interaction with the bilayer precedes SERCA binding and may mediate the interactions with other proteins such as protein kinase A and protein phosphatase 1. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 37 |
| Volume Number | 104 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2007-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Calcium-Binding Proteins Chemistry Mass Spectrometry Membrane Proteins Animals Isolation & Purification Computer Simulation Electron Spin Resonance Spectroscopy Escherichia Coli Metabolism Lipid Bilayers Micelles Models, Molecular Molecular Weight Nuclear Magnetic Resonance, Biomolecular Phosphatidylcholines Phosphatidylethanolamines Protein Structure, Secondary Rabbits Reproducibility Of Results Sarcoplasmic Reticulum Calcium-Transporting ATPases Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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