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Titolo:
Ligand induced conformational states of the 5-HT1A receptor
Autore:
Sylte, I; Bronowska, A; Dahl, SG;
Indirizzi:
Univ Tromso, Fac Med, Inst Med Biol, Dept Pharmacol, N-9037 Tromso, NorwayUniv Tromso Tromso Norway N-9037 , Dept Pharmacol, N-9037 Tromso, Norway Univ Warsaw, Dept Chem, PL-02093 Warsaw, Poland Univ Warsaw Warsaw Poland PL-02093 w, Dept Chem, PL-02093 Warsaw, Poland
Titolo Testata:
EUROPEAN JOURNAL OF PHARMACOLOGY
fascicolo: 1-2, volume: 416, anno: 2001,
pagine: 33 - 41
SICI:
0014-2999(20010323)416:1-2<33:LICSOT>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-COUPLED RECEPTORS; MOLECULAR-DYNAMICS; 5-HT(1A) RECEPTOR; TRANSMEMBRANE HELICES; BUSPIRONE ANALOGS; ALPHA-SUBUNITS; BINDING SITE; ACTIVATION; RHODOPSIN; RESIDUES;
Keywords:
G-protein coupled receptor; molecular dynamics; receptor activation; conformational changes; ligand induced;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Sylte, I Univ Tromso, Fac Med, Inst Med Biol, Dept Pharmacol, N-9037 Tromso, Norway Univ Tromso Tromso Norway N-9037 armacol, N-9037 Tromso, Norway
Citazione:
I. Sylte et al., "Ligand induced conformational states of the 5-HT1A receptor", EUR J PHARM, 416(1-2), 2001, pp. 33-41

Abstract

It has been shown that G-protein coupled receptors have seven transmembrane alpha -helices, but the structural changes occurring in a G-protein coupled receptor as a response on agonist stimulus and the molecular events leading to blockade of the signal transduction by antagonists are not well understood. In the present study, the AMBER 5.0 force field was used for comparative molecular dynamics simulations of a 5-HT1A receptor model in the absence of ligand, in complex with a 5-HT1A receptor agonist (R)-8-hydroxy-2-(di-n-propylamino)tetralin [(R)-8-OH-DPAT], in complex with a selective 5-HT1A receptor antagonist (S)-N-rert-butyl-3-[4-(2-methoxyphenyl)piperazin-1-yl]-2-phenylpropanamide [(S)-WAY100135], and in complex with the partial agonist, buspirone. In the simulations, the agonist induced larger conformational changes into transmembrane helix 3 and 6 than into the other helices, while the main conformational differences between the agonist bound receptorand the antagonist bound receptor were in transmembrane helix 5 and 6. During the simulations, all the three ligands constrained the helical movements compared to those observed in the receptor without any ligand. (C) 2001 Elsevier Science B.V. All rights reserved.

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Documento generato il 29/09/20 alle ore 07:40:58