Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Ligand Docking Methods to Recognize Allosteric Inhibitors for G-protein Coupled Receptors

Version 1 : Received: 28 November 2020 / Approved: 3 December 2020 / Online: 3 December 2020 (13:08:24 CET)

How to cite: Harini, K.; Jayashree, S.; Tiwari, V.; Vishwanath, S.; Sowdhamini, R. Ligand Docking Methods to Recognize Allosteric Inhibitors for G-protein Coupled Receptors. Preprints 2020, 2020120085 (doi: 10.20944/preprints202012.0085.v1). Harini, K.; Jayashree, S.; Tiwari, V.; Vishwanath, S.; Sowdhamini, R. Ligand Docking Methods to Recognize Allosteric Inhibitors for G-protein Coupled Receptors. Preprints 2020, 2020120085 (doi: 10.20944/preprints202012.0085.v1).

Abstract

G-protein coupled receptors (GPCRs) are large protein families known to be important in many cellular processes. They are well known for their allosteric activation mechanisms. They are drug targets for several FDA-approved drugs. We have investigated the diversity of the ligand binding site for these class of proteins against their cognate ligands using computational docking, even if their structures are known 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. Further, ligands obtained from GLASS database, which consists of experimentally verified GPCR ligands, also show allosteric binding to GPCRs. The allosteric binders show strong affinity to the binding site, though the residues at the binding site are not conserved across GPCR subfamilies.

Subject Areas

allosteric ligands; AutoDock; cognate ligands; Tanimoto co-efficient; GPCRs

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