An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes.
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ABSTRACT:
SUBMITTER: Lian P
PROVIDER: S-EPMC3078132 | biostudies-literature | 2011
REPOSITORIES: biostudies-literature
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An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes.
Lian Peng P Wei Dong-Qing DQ Wang Jing-Fang JF Chou Kuo-Chen KC
PloS one 20110415 4
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" ...[more]
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