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Titolo:
INTERACTION OF D-TUBOCURARINE ANALOGS WITH THE 5HT(3) RECEPTOR
Autore:
YAN D; PEDERSEN SE; WHITE MM;
Indirizzi:
ALLEGHENY UNIV HLTH SCI,DEPT PHARMACOL,3200 HENRY AVE PHILADELPHIA PA19129 ALLEGHENY UNIV HLTH SCI,DEPT PHARMACOL PHILADELPHIA PA 19129 BAYLOR COLL MED,DEPT MOL PHYSIOL & BIOPHYS HOUSTON TX 77030
Titolo Testata:
Neuropharmacology
fascicolo: 2, volume: 37, anno: 1998,
pagine: 251 - 257
SICI:
0028-3908(1998)37:2<251:IODAWT>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
NICOTINIC ACETYLCHOLINE-RECEPTOR; GATED ION-CHANNEL; SUBUNIT INTERFACES; FUNCTIONAL EXPRESSION; MOLECULAR DISSECTION; ALPHA-GAMMA; BINDING; (+)-TUBOCURARINE; IDENTIFICATION; SELECTIVITY;
Keywords:
5-HT; 5-HT3 RECEPTOR; D-TURBOCURARINE ANALOGS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
20
Recensione:
Indirizzi per estratti:
Citazione:
D. Yan et al., "INTERACTION OF D-TUBOCURARINE ANALOGS WITH THE 5HT(3) RECEPTOR", Neuropharmacology, 37(2), 1998, pp. 251-257

Abstract

D-Tubocurarine is a potent competitive antagonist of two members of the ligand-gated ion channel family, the muscle-type nicotinic acetylcholine receptor (AChR) and serotonin type-3 receptor (5HT(3)R). We haveused a series of analogs of D-tubocurarine to determine the effects of methylation, stereoisomerization and halogenation on the interactionof D-tubocurarine with the 5HT(3)R. The affinities of the analogs forthe 5HT(3)R span a 200-fold concentration range and fall into three broad groups. The first group, with affinity constants (K-i) < 150 nM, consists of D-tubocurarine and analogs modified at the nitrogens or 7'hydroxyl. The fact that these compounds all have high affinity for the 5HT(3)R suggests that these portions of the ligand do not make interactions with the receptor that are critical for high-affinity binding. The second group, with K-i's in the 1-5 mu M range, consists of analogs modified at the 12'-hydroxyl or the adjacent 13'-carbon, which suggests that this portion of the ligand makes interactions that are important for high-affinity binding. The third, very low affinity, group isa compound with altered stereoconfiguration at the 1 carbon, demonstrating the importance of proper configuration of the antagonist in ligand-receptor interactions. For the most part, this pattern of selectivity is similar to that for the AChR, suggesting that the structures of the ligand-binding sites of these two receptors share common structural features. (C) 1998 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 00:26:46