Harini, K and Jayashree, S and Tiwari, V and Vishwanath, S and Sowdhamini, R (2021) Ligand Docking Methods to Recognize Allosteric Inhibitors for G-Protein-Coupled Receptors. In: Bioinformatics and Biology Insights, 15 .
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Abstract
G-protein-coupled receptors (GPCRs) are membrane proteins which play an important role in many cellular processes and are excellent drug targets. Despite the existence of several US Food and Drug Administration (FDA)-approved GPCR-targeting drugs, there is a continuing challenge of side effects owing to the nonspecific nature of drug binding. We have investigated the diversity of the ligand binding site for this class of proteins against their cognate ligands using computational docking, even if their structures are known already in the ligand-complexed form. The cognate ligand of some of these receptors dock at allosteric binding site with better score than the binding at the conservative site. Interestingly, amino acid residues at such allosteric binding site are not conserved across GPCR subfamilies. Such a computational approach can assist in the prediction of specific allosteric binders for GPCRs. © The Author(s) 2021.
| Item Type: | Journal Article |
|---|---|
| Publication: | Bioinformatics and Biology Insights |
| Publisher: | SAGE Publications Inc. |
| Additional Information: | The copyright for this article belongs to SAGE Publications Inc. |
| Keywords: | beta 2 adrenergic receptor; chemokine receptor; chemokine receptor CXCR4; drug; G protein coupled receptor; serotonin 2B receptor, allosterism; Article; binding site; drug targeting; hydrogen bond; ligand binding; molecular docking; molecular dynamics; sequence alignment |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
| Date Deposited: | 17 Nov 2021 10:00 |
| Last Modified: | 17 Nov 2021 10:00 |
| URI: | http://eprints.iisc.ac.in/id/eprint/70513 |
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