How well can molecular modelling predict the crystal structure: the case of the ligand-binding domain of glutamate receptors.
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.
Paas
Y
Y
Unité de Neurobiologie Moléculaire, CNRS UA D1284, Institut Pasteur, 25 Rue du Dr Roux, 75015 Paris, France. ypaas@pasteur.fr
Devillers-Thiéry
A
A
Teichberg
V I
VI
Changeux
J P
JP
Eisenstein
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011237:Predictive Value of Tests; D017470:Receptors, Glutamate / Q000737:chemistry* / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
D008024:Ligands; D017470:Receptors, Glutamate