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...

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Bibliographic Details
Published in:PloS one 2011-04, Vol.6 (4), p.e18587-e18587
Main Authors: Lian, Peng, Wei, Dong-Qing, Wang, Jing-Fang, Chou, Kuo-Chen
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Allosteric properties
Allosteric Regulation
Analysis
ATPases
Biological activity
Biology
Ca2+-transporting ATPase
Calcium (reticular)
Calcium-Binding Proteins - chemistry
Cardiac muscle
Chemistry
Cytoplasm - chemistry
Dynamic structural analysis
Electrolytes
Heart
Heart diseases
Kinases
Laboratories
Life sciences
Lipid Bilayers - chemistry
Lipid membranes
Lipids
Membranes
Metabolism
Molecular dynamics
Molecular Dynamics Simulation
NMR
Nuclear magnetic resonance
Phospholamban
Phosphorylation
Protein Multimerization
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Sarcoplasmic reticulum
Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism
Simulation
Studies
Trajectory analysis
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0018587