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Molecular dynamics simulation involved in expounding the activation of adrenoceptors by sympathetic nervous system signaling

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Abstract

G-protein–coupled receptors are integral membrane proteins involved in signal transduction pathways, making them an appealing drug targets for a wide spectrum of diseases. The previous literature reports provide an evidence that catecholamine regulates metastasis by actuating the β2-adrenergic receptor (β-2AR). Molecular dynamics simulations were carried out for 1000 ns to understand the effect of the catecholamine on the human β-2AR. On comparing the apoprotein structure of β-2AR with that of catecholamine interacted β-2AR protein, a large change in structural assembly is observed in the helical regions which confirm the activation of β-2AR protein. The visualization of internal natural pathway of β-2AR protein structure gives us detailed information about deviation in TM helixes. The compactness of protein structure shows β-2AR protein interacting with epinephrine is much stable than β-2AR protein interacting with norepinephrine structure. The Gibbs free energy shows norepinephrine as a partial agonist whereas epinephrine as full agonist for β-2AR protein.

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Abbreviations

GPCRs:

G-protein coupled receptors

SNS:

Sympathetic nervous system

MD:

Molecular dynamics

β-2AR:

β2-adrenergic receptor

TM:

Transmembrane

CNS:

Central nervous system

RMSD:

Root mean square deviation

RMSF:

Root mean square fluctuation

Rg:

Radius of gyration

SASA:

Solvent accessible surface area

FEL:

Free energy landscape

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I Rahul Suresh, express my sincere thanks to DST-PURSE for the financial assistant provided during this course of work.

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  1. Department of Physics, Bharathiar University, Coimbatore, India

    Rahul Suresh

  2. Department of Medical Physics, Bharathiar University, Coimbatore, India

    Vijayakumar Subramaniam

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Suresh, R., Subramaniam, V. Molecular dynamics simulation involved in expounding the activation of adrenoceptors by sympathetic nervous system signaling. Struct Chem 31, 1869–1885 (2020). https://doi.org/10.1007/s11224-020-01553-5

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