Ligand Docking Methods to Recognize Allosteric Inhibitors for G-Protein-Coupled Receptors.
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Publication Date
2021Journal Title
Bioinform Biol Insights
ISSN
1177-9322
Publisher
SAGE Publications
Volume
15
Language
eng
Type
Article
This Version
VoR
Metadata
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Harini, K., Jayashree, S., Tiwari, V., Vishwanath, S., & Sowdhamini, R. (2021). Ligand Docking Methods to Recognize Allosteric Inhibitors for G-Protein-Coupled Receptors.. Bioinform Biol Insights, 15 https://doi.org/10.1177/11779322211037769
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.
Keywords
Autodock, G-protein-coupled Receptors, Allosteric Ligands, Cognate Ligands, Tanimoto Co-Efficient
Identifiers
PMC8558589, 34733103
External DOI: https://doi.org/10.1177/11779322211037769
This record's URL: https://www.repository.cam.ac.uk/handle/1810/332223
Rights
Attribution-NonCommercial 4.0 International
Licence URL: https://creativecommons.org/licenses/by-nc/4.0/
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