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Structural Determinants of the Neuronal Glycine Transporter 2 for the Selective Inhibitors ALX1393 and ORG25543

Cristina Benito-Muñoz, Almudena Perona, Raquel Felipe, Gonzalo Pérez‐Siles, Enrique Núñez, Carmen Aragón, Beatriz López‐Corcuera

2021ACS Chemical Neuroscience12 citationsDOIOpen Access PDF

Abstract

. Molecular dynamics simulations and energy analysis of the complex and functional analysis of a series of point mutants permitted to determine the structural determinants of ALX1393 and ORG25543 discrimination by GlyT2. The ligands establish simultaneous contacts with residues present in transmembrane domains 1, 3, 6, and 8 and block the transporter in outward-facing conformation and hence inhibit glycine transport. In addition, differential interactions of ALX1393 with the cation bound at Na1 site and ORG25543 with TM10 define the differential sites of the inhibitors and explain some of their individual features. Structural information about the interactions with GlyT2 may provide useful tools for new drug discovery.

Topics & Concepts

Glycine receptorNeurotransmissionNeuroscienceNeurotransmitter transporterTransporterChemistryBiologyGlycinePharmacologyNeurotransmitterBiochemistryReceptorAmino acidCentral nervous systemGeneNeuroscience and Neuropharmacology ResearchReceptor Mechanisms and SignalingIon channel regulation and function