alexa Homology Modelling and Docking Studies of Human α2-Adrenergic Receptor Subtypes
ISSN: 0974-7230

Journal of Computer Science & Systems Biology
Open Access

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Research Article

Homology Modelling and Docking Studies of Human α2-Adrenergic Receptor Subtypes

Archana Jayaraman, Kaiser Jamil and Kavita K Kakarala*

Centre for Biotechnology and Bioinformatics (CBB), School of Life Sciences, Jawaharlal Nehru Institute of Advanced Studies (JNIAS), Secunderabad, Andhra Pradesh, India

*Corresponding Author:
Dr. Kavita Kumari K
Centre for Biotechnology and Bioinformatics (CBB)
School of Life Sciences, Jawaharlal Nehru Institute of Advanced Studies (JNIAS)
6th Floor, Buddha Bhawan, M G Road
Secunderabad-500003, Andhra Pradesh, India
E-mail: [email protected]

Received date: May 06, 2013; Accepted date: June 24, 2013; Published date: June 26, 2013

Citation: Jayaraman A, Jamil K, Kakarala KK (2013) Homology Modelling and Docking Studies of Human a2-Adrenergic Receptor Subtypes. J Comput Sci Syst Biol 6:136-149. doi:10.4172/jcsb.1000111

Copyright: © 2013 Jayaraman A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License,which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

α2-adrenergic receptors play a key role in the regulation of sympathetic system, neurotransmitter release, blood pressure and intraocular pressure. Although α2-adrenergic receptors mediate a number of physiological functions in vivo and have great therapeutic potential, the absence of crystal structure of α2-adrenergic receptor subtypes is a major hindrance in the drug design efforts. The therapeutic efficacy of the available drugs is not selective for subtype specificity (α2a, α2b and α2c) leading to unwanted side effects. We used Homology modelling and docking studies to understand and analyze the residues important for agonist and antagonist binding. We have also analyzed binding site volume, and the residue variations which may play important role in ligand binding. We have identified residues through our modelling and docking studies, which would be critical in giving subtype specificity and may help in the development of future subtype-selective drugs.

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