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Titolo:
Allosteric interaction between the amino terminal domain and the ligand binding domain of NR2A
Autore:
Zheng, F; Erreger, K; Low, CM; Banke, T; Lee, CJ; Conn, PJ; Traynelis, SF;
Indirizzi:
Emory Univ, Sch Med, Dept Pharmacol, Atlanta, GA 30322 USA Emory Univ Atlanta GA USA 30322 ed, Dept Pharmacol, Atlanta, GA 30322 USA
Titolo Testata:
NATURE NEUROSCIENCE
fascicolo: 9, volume: 4, anno: 2001,
pagine: 894 - 901
SICI:
1097-6256(200109)4:9<894:AIBTAT>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
D-ASPARTATE RECEPTORS; CALCIUM-DEPENDENT INACTIVATION; GLYCINE-INSENSITIVE DESENSITIZATION; CULTURED HIPPOCAMPAL-NEURONS; OUTSIDE-OUT PATCHES; NMDA RECEPTOR; ZINC INHIBITION; NR1 SUBUNIT; CHANNELS; AFFINITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Zheng, F Emory Univ, Sch Med, Dept Pharmacol, 1510 Clifton Rd, Atlanta, GA30322 USA Emory Univ 1510 Clifton Rd Atlanta GA USA 30322 nta, GA 30322 USA
Citazione:
F. Zheng et al., "Allosteric interaction between the amino terminal domain and the ligand binding domain of NR2A", NAT NEUROSC, 4(9), 2001, pp. 894-901

Abstract

Fast desensitization is an important regulatory mechanism of neuronal NMDAreceptor function. Only recombinant NMDA receptors composed of NR1/NR2A exhibit a fast component of desensitization similar to neuronal NMDA receptors. Here we report that the fast desensitization of NR1/NR2A receptors is caused by ambient zinc, and that a positive allosteric interaction occurs between the extracellular zinc-binding site located in the amino terminal domain and the glutamate-binding domain of NR2A. The relaxation of macroscopic currents reflects a shift to a new equilibrium due to increased zinc affinity after binding of glutamate. We also show a similar interaction between the ifenprodil binding site and the glutamate binding site of NR1/NR2B receptors. These data raise the possibility that there is an allosteric interaction between the amino terminal domain and the ligand-binding domain of other glutamate receptors. Our findings may provide insight into how zinc and other extracellular modulators regulate NMDA receptor function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 16:20:26