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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sayadi, Maryam Feig, Michael |
| Description | Author Affiliation: Sayadi M ( Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA.) |
| Abstract | Phosphorylation of phospholamban (PLB) at Ser16 and/ or Thr17 is believed to release its inhibitory effect on sarcoplasmic reticulum calcium ATPase. Ser16 phosphorylation of PLB has been suggested to cause a conformational change that alters the interaction between the enzyme and protein. Using computer simulations, the conformational sampling of Ser16 phosphorylated PLB in implicit membrane environment is compared here with the unphosphorylated PLB system to investigate these conformational changes. The results suggest that conformational changes in the cytoplasmic domain of PLB upon phosphorylation at Ser16 increase the likelihood of unfavorable interactions with SERCA in the E2 state prompting a conformational switch of SERCA from E2 to E1. Phosphorylation of PLB at Thr17 on the other hand does not appear to affect interactions with SERCA significantly suggesting that the mechanism of releasing the inhibitory effect is different between Thr17 phosphorylated and Ser16 phosphorylated PLB. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 2 |
| Volume Number | 1828 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2013-02-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Calcium-Binding Proteins Chemistry Sarcoplasmic Reticulum Calcium-Transporting ATPases Serine Threonine Animals Cell Membrane Metabolism Computer Simulation Cytoplasm Models, Molecular Molecular Conformation Molecular Dynamics Simulation Phosphorylation Protein Binding Protein Conformation Protein Structure, Tertiary Rabbits Research Support, U.S. Gov't, Non-P.H.S. Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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