« Previous Abstract"Components of the Female Sex Pheromone of the Newly-Described Canola Flower Midge, Contarinia brassicola"    Next Abstract"Isolation and identification of 9-methylgermacrene-B as the putative sex pheromone of Lutzomyia cruzi (Mangabeira, 1938) (Diptera: Psychodidae)" »

Sci Rep

Title:		Ligand-Induced Conformational Dynamics of A Tyramine Receptor from Sitophilus oryzae
Author(s):		Braza MKE; Gazmen JDN; Yu ET; Nellas RB;
Address:		"Institute of Chemistry, College of Science, University of the Philippines Diliman, Quezon City, 1101, Philippines. Institute of Chemistry, College of Science, University of the Philippines Diliman, Quezon City, 1101, Philippines. rbnellas@up.edu.ph"
Journal Title:		Sci Rep
Year:		2019
Volume:		20191107
Issue:		1
Page Number:		16275 -
DOI:		10.1038/s41598-019-52478-x
ISSN/ISBN:		2045-2322 (Electronic) 2045-2322 (Linking)
Abstract:		"Tyramine receptor (TyrR) is a biogenic amine G protein-coupled receptor (GPCR) associated with many important physiological functions in insect locomotion, reproduction, and pheromone response. Binding of specific ligands to the TyrR triggers conformational changes, relays the signal to G proteins, and initiates an appropriate cellular response. Here, we monitor the binding effect of agonist compounds, tyramine and amitraz, to a Sitophilus oryzae tyramine receptor (SoTyrR) homology model and their elicited conformational changes. All-atom molecular dynamics (MD) simulations of SoTyrR-ligand complexes have shown varying dynamic behavior, especially at the intracellular loop 3 (IL3) region. Moreover, in contrast to SoTyrR-tyramine, SoTyrR-amitraz and non-liganded SoTyrR shows greater flexibility at IL3 residues and were found to be coupled to the most dominant motion in the receptor. Our results suggest that the conformational changes induced by amitraz are different from the natural ligand tyramine, albeit being both agonists of SoTyrR. This is the first attempt to understand the biophysical implication of amitraz and tyramine binding to the intracellular domains of TyrR. Our data may provide insights into the early effects of ligand binding to the activation process of SoTyrR"
Keywords:		"Animals Binding Sites Coleoptera Humans *Ligands *Molecular Conformation *Molecular Docking Simulation *Molecular Dynamics Simulation Protein Binding Receptors, Biogenic Amine/*chemistry/metabolism Tyramine/*chemistry/metabolism;"
Notes:		"MedlineBraza, Mac Kevin E Gazmen, Jerrica Dominique N Yu, Eizadora T Nellas, Ricky B eng Research Support, Non-U.S. Gov't England 2019/11/09 Sci Rep. 2019 Nov 7; 9(1):16275. doi: 10.1038/s41598-019-52478-x"