How well can molecular modelling predict the crystal structure: the case of the ligand-binding domain of glutamate receptors
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Updated: Oct 17, 2026

Modeling Ligands into Maps Derived from Electron Cryomicroscopy
Published on: July 19, 2024
Y Paas1, A Devillers-Thiéry, V I Teichberg
1Unité de Neurobiologie Moléculaire, CNRS UA D1284, Institut Pasteur, 25 Rue du Dr Roux, 75015 Paris, France. ypaas@pasteur.fr
Abstract:
The concept that the ligand-binding domain of vertebrate glutamate receptor channels and bacterial periplasmic substrate-binding proteins (PBPs) share similar three-dimensional (3D) structures has gained increasing support in recent years. On the basis of a dual approach that included computer-assisted molecular modelling and functional studies of site-specific mutants, theoretical 3D models of this domain have been proposed. This article reviews to what extent these models could predict the crystal structure of the ligand-binding domain of an ionotropic glutamate receptor subunit recently determined at high resolution by X-ray diffraction studies.
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