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Structure–Function Prediction of $alpha$2A-, $alpha$2B-, and $alpha$2C-Adrenoceptors using Homology Model Assisted Antagonist Binding Study

Publication Type : Journal Article

Thematic Areas : Nanosciences and Molecular Medicine

Publisher : Medicinal Chemistry Research

Source : Medicinal Chemistry Research, Volume 23, Number 2, p.735–746 (2014)

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Campus : Kochi

School : Center for Nanosciences

Center : Amrita Center for Nanosciences and Molecular Medicine Move, Nanosciences

Department : Nanosciences and Molecular Medicine

Year : 2014

Abstract : $alpha$2A-, $alpha$2B-, and $alpha$2C-adrenoceptors belong to the rhodopsin-like G-protein coupled receptors family. They are integral membrane proteins typified by a bundle of seven transmembrane helices. 50nbsp;{%} of the currently available drugs in the market target G-protein coupled receptors. Crystal structure of $alpha$2A-, $alpha$2B-, and $alpha$2C-adrenoceptors are not yet solved. We performed homology modeling of the human $alpha$2A-, $alpha$2B-, and $alpha$2C-adrenoceptor subtypes based on the crystal structure of the $beta$2-adrenergic receptor. Molecular docking studies of five different antagonists toward these receptors revealed receptor subtype selectivity, and which in turn potentially guide in the rational design of subtype selective antagonists.

Cite this Research Publication : V. Kumar, Bansal, G., Patel, J., and Dr. Gopi Mohan C., “Structure–Function Prediction of $\alpha$2A-, $\alpha$2B-, and $\alpha$2C-Adrenoceptors using Homology Model Assisted Antagonist Binding Study”, Medicinal Chemistry Research, vol. 23, pp. 735–746, 2014.

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