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• W2008593197 abstract "G-protein-coupled receptors (GPCRs) are membrane proteins that have a wide variety of physiological roles. Adenosine receptors belong to the GPCR family. Adenosine receptors are implicated in many physiological disorders, such as Parkinson's disease, Huntington's disease, inflammatory and immune's disease and many others. Interestingly, crystal structures of the active and inactive conformations of the A2-subtype adenosine receptor (A2AR) have been solved. These two structures could be used to get insights about the conformational changes that occur during the process of activation/inactivation processes of this receptor. Therefore, two ligand-free simulations of the native active (PDB code: 3QAK) and inactive (PDB code: 3EML) conformations of the A2AR and two halo-simulations were carried out to observe the initial conformational changes induced by coupling adenosine to the inactive conformation and caffeine to the active conformation. Furthermore, we constructed an A2AR model that contained four thermostabilising mutations, L48A, T65A, Q89A and A54L, which had previously been determined to stabilise the bound conformation of the agonist, and we ran molecular dynamics simulations of this mutant to investigate how these point mutations might affect the inactive conformation of this receptor. This study provides insights about the initial structural and dynamic features that occur as a result of the binding of caffeine and adenosine in the active and inactive A2AR structures, respectively, as well as the introduction of some mutations on the inactive structure of the A2AR. Moreover, we provide useful and detailed information regarding structural features such as toggle switch and ionic lock during the activation/inactivation processes of this receptor." @default.
• W2008593197 created "2016-06-24" @default.
• W2008593197 creator A5033283009 @default.
• W2008593197 creator A5041724997 @default.
• W2008593197 date "2013-09-23" @default.
• W2008593197 modified "2023-09-23" @default.
• W2008593197 title "Molecular dynamics simulations reveal initial structural and dynamic features for the A₂AR as a result of ligand binding" @default.
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• W2008593197 doi "https://doi.org/10.1080/08927022.2013.835485" @default.
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