The macro- and microarchitectures of the ligand-binding domain of glutamate receptors.
Over the last decade, a large body of information regarding the amino acid sequences and tertiary structures of many proteins has accumulated. Subtle similarities in sequence patterns identified between glutamate receptors and bacterial periplasmic substrate-binding proteins have suggested that structural kinship exists between these protein families. Many of the bacterial periplasmic binding proteins but none of the glutamate receptors have been crystallized so far. The following article reviews how the resemblance between these two protein families led to computer-assisted structural models of crucial elements involved in ligand binding by various glutamate receptors. A plausible dynamic model of the molecular mechanism of activation and desensitization of glutamate-receptor channels is also discussed.
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Neurobiologie Moléculaire, UA CNRS D1284, Département des Biotechnologies, Institut Pasteur, Paris, France.
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008024:Ligands; D008961:Models, Structural; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D018091:Receptors, AMPA / Q000235:genetics / Q000378:metabolism; D017470:Receptors, Glutamate / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D008024:Ligands; D018091:Receptors, AMPA; D017470:Receptors, Glutamate