An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes.
Phospholamban functions as a regulator of Ca(2+) concentration of cardiac muscle cells by triggering the bioactivity of sarcoplasmic reticulum Ca(2+)-ATPase. In order to understand its dynamic mechanism in the environment of bilayer surroundings, we performed long time-scale molecular dynamic simula...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2011-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3078132?pdf=render |
| _version_ | 1819266617888997376 |
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| author | Peng Lian Dong-Qing Wei Jing-Fang Wang Kuo-Chen Chou |
| author_facet | Peng Lian Dong-Qing Wei Jing-Fang Wang Kuo-Chen Chou |
| author_sort | Peng Lian |
| collection | DOAJ |
| description | Phospholamban functions as a regulator of Ca(2+) concentration of cardiac muscle cells by triggering the bioactivity of sarcoplasmic reticulum Ca(2+)-ATPase. In order to understand its dynamic mechanism in the environment of bilayer surroundings, we performed long time-scale molecular dynamic simulations based on the high-resolution NMR structure of phospholamban pentamer. It was observed from the molecular dynamics trajectory analyses that the conformational transitions between the "bellflower" and "pinwheel" modes were detected for phospholamban. Particularly, the two modes became quite similar to each other after phospholamban was phosphorylated at Ser16. Based on these findings, an allosteric mechanism was proposed to elucidate the dynamic process of phospholamban interacting with Ca(2+)-ATPase. |
| first_indexed | 2024-12-23T21:04:08Z |
| format | Article |
| id | doaj.art-a5587d2f9eeb43ce97403d3a453cc0e9 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-23T21:04:08Z |
| publishDate | 2011-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-a5587d2f9eeb43ce97403d3a453cc0e92022-12-21T17:31:17ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-0164e1858710.1371/journal.pone.0018587An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes.Peng LianDong-Qing WeiJing-Fang WangKuo-Chen ChouPhospholamban functions as a regulator of Ca(2+) concentration of cardiac muscle cells by triggering the bioactivity of sarcoplasmic reticulum Ca(2+)-ATPase. In order to understand its dynamic mechanism in the environment of bilayer surroundings, we performed long time-scale molecular dynamic simulations based on the high-resolution NMR structure of phospholamban pentamer. It was observed from the molecular dynamics trajectory analyses that the conformational transitions between the "bellflower" and "pinwheel" modes were detected for phospholamban. Particularly, the two modes became quite similar to each other after phospholamban was phosphorylated at Ser16. Based on these findings, an allosteric mechanism was proposed to elucidate the dynamic process of phospholamban interacting with Ca(2+)-ATPase.http://europepmc.org/articles/PMC3078132?pdf=render |
| spellingShingle | Peng Lian Dong-Qing Wei Jing-Fang Wang Kuo-Chen Chou An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes. PLoS ONE |
| title | An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes. |
| title_full | An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes. |
| title_fullStr | An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes. |
| title_full_unstemmed | An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes. |
| title_short | An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes. |
| title_sort | allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes |
| url | http://europepmc.org/articles/PMC3078132?pdf=render |
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