Publication Type:

Journal Article

Source:

Medicinal Chemistry Research, Volume 23, Number 2, p.735-746 (2014)

URL:

https://www.scopus.com/inward/record.url?eid=2-s2.0-84893800918&partnerID=40&md5=e38b7398b19fb2394ee314f94c4acc54

Keywords:

2 (1 methyl 2 isoindolinylmethyl) 2 imidazoline, 2 [2 [4 (2 methoxyphenyl) 1 piperazinyl]ethyl] 4, 2 [[2 (2, 3(2h, 4 benzodioxan, 4 dimethyl 1, 4h) isoquinolinedione, 6 dimethoxyphenoxy)ethyl]aminomethyl] 1, alpha 2A adrenergic receptor, alpha 2B adrenergic receptor, alpha 2C adrenergic receptor, alpha adrenergic receptor blocking agent, amino acid sequence, article, binding affinity, binding site, carazolol, carvedilol, chlorpromazine, crystal structure, drug protein binding, drug structure, hydrogen bond, molecular docking, molecular model, prediction, Protein Structure, Sequence Alignment, structure activity relation, yohimbine

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.

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, vol. 23, pp. 735-746, 2014.