THE MACROARCHITECTURES 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 accumulate d. Subtle similarities in sequence patterns identified between glutama te receptors and bacterial periplasmic substrate-binding proteins have suggested that structural kinship exists between these protein famili es. Many of the bacterial periplasmic binding proteins but none of the glutamate receptors have been crystallized so far. The following arti cle reviews how the resemblance between these two protein families led to computer-assisted structural models of crucial elements involved i n ligand binding by various glutamate receptors. A plausible dynamic m odel of the molecular mechanism of activation and desensitization of g lutamate-receptor channels is also discussed.