Publication Type:

Journal Article

Source:

Medicinal Chemistry Research, p.1-12 (2013)

URL:

http://www.scopus.com/inward/record.url?eid=2-s2.0-84878893627&partnerID=40&md5=bc3cfc36f8a884ecb00bfd31f425dfef

Abstract:

Abstract: α2A-, α2B-, and α2C-adrenoceptors belong to the rhodopsin-like G-protein coupled receptors family. They are integral membrane proteins typified by a bundle of seven transmembrane helices. 50 % of the currently available drugs in the market target G-protein coupled receptors. Crystal structure of α2A-, α2B-, and α2C-adrenoceptors are not yet solved. We performed homology modeling of the human α2A-, α2B-, and α2C-adrenoceptor subtypes based on the crystal structure of the β2-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. Graphical Abstract: [Figure not available: see fulltext.] © 2013 Springer Science+Business Media New York.

Notes:

cited By (since 1996)0; Article in Press

Cite this Research Publication

Va Kumar, Bansal, Ga, Patel, Ja, and Mohan, Cab Gopi, “Structure-function prediction of α2A-, α2B-, and α2C-adrenoceptors using homology model assisted antagonist binding study”, Medicinal Chemistry Research, pp. 1-12, 2013.

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