title: Molecular dynamics simulation of the ligand binding domain of mGluR1 in response to agonist and antagonist binding.
abstract: The interdomain movements of the ligand binding domain (LBD) of mGluR1 in response to agonist or antagonist binding are studied by 2 ns molecular dynamics (MD) simulations. Our results indicate that MD is able to reproduce many of the experimentally determined features of the open and closed conformations of LBD. Analysis of the ligand behavior over time allows to delineate some of the molecular determinants responsible for the agonist-induced or antagonist-blocked LBD responses.
authors.affiliation: Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Via del Liceo 1, 06123 Perugia, Italy. gabri@unipg.it
authors.forename: Gabriele
authors.initials: G
authors.lastname: Costantino
authors.forename: Antonio
authors.initials: A
authors.lastname: Macchiarulo
authors.forename: Maxim
authors.initials: M
authors.lastname: Belenikin
authors.forename: Roberto
authors.initials: R
authors.lastname: Pellicciari
mesh_terms: D001665:Binding Sites; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D066298:In Vitro Techniques; D008024:Ligands; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D018094:Receptors, Metabotropic Glutamate / Q000819:agonists / Q000037:antagonists & inhibitors / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D008024:Ligands; D018094:Receptors, Metabotropic Glutamate; C104077:metabotropic glutamate receptor type 1