Publication

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.