Characterization of Membranal and Purified NMDA Receptors
Over the past years considerable progress has been made towards understanding the biochemical and physiological significance of the N-methyl-D-aspartate (NMDA) type of excitatory amino acid receptor (for review see Cotman & Iversen, 1987). Receptor binding and electrophysiological studies have indicated that the NMDA-receptor complex comprises a number of distinct structural domains through which its function may be regulated or pharmacologically modified. The domains identified so far are: (i) the glutamate-binding site; (ii) an allosteric site, where glycine and/or 1-aminocyclopropane-l-carboxylic acid (ACC) regulate agonist-induced channel opening; (iii) a site (or sites) through which Mg2+ modulates the passage of ions; (iv) a site or sites that recognizes Zn2+ and prevents channel activation, and (v) a site or sites within the receptor channel for binding of drugs such as phencyclidine (PCP)-like, MK-801 and ketamine.
KeywordsNMDA Receptor Sodium Cholate Excitatory Amino Acid Receptor Photoaffinity Label Label Ligand
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