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Titolo:
A computational model of the 5-HT3 receptor extracellular domain: search for ligand binding sites
Autore:
Menziani, MC; De Rienzo, F; Cappelli, A; Anzini, M; De Benedetti, PG;
Indirizzi:
Univ Modena & Reggio E, Dipartimento Chim, I-41100 Modena, Italy Univ Modena & Reggio E Modena Italy I-41100 Chim, I-41100 Modena, Italy Univ Siena, Dipartimento Farmaco Chim Tecnol, I-53100 Siena, Italy Univ Siena Siena Italy I-53100 Farmaco Chim Tecnol, I-53100 Siena, Italy Univ Catanzaro Magna Graecia, Dipartimento Sci Farmaco Biol, I-88021 Catanzaro, Italy Univ Catanzaro Magna Graecia Catanzaro Italy I-88021 21 Catanzaro, Italy
Titolo Testata:
THEORETICAL CHEMISTRY ACCOUNTS
fascicolo: 1-2, volume: 106, anno: 2001,
pagine: 98 - 104
SICI:
1432-881X(200106)106:1-2<98:ACMOT5>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
NICOTINIC ACETYLCHOLINE-RECEPTOR; INHIBITORY GLYCINE RECEPTOR; DIFFERENT INTRINSIC EFFICACY; ION-CHANNEL RECEPTORS; ARYLPIPERAZINE DERIVATIVES; SECONDARY STRUCTURE; DISULFIDE LOOP; SUBUNIT; POTENT; ORIENTATION;
Keywords:
molecular modelling; 5-HT3 receptor; extracellular domain; ligand binding site; ligand-gated ion channel;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Menziani, MC Univ Modena & Reggio E, Dipartimento Chim, Via Campi 183, I-41100 Modena, Italy Univ Modena & Reggio E Via Campi 183 Modena Italy I-41100 ly
Citazione:
M.C. Menziani et al., "A computational model of the 5-HT3 receptor extracellular domain: search for ligand binding sites", THEOR CH AC, 106(1-2), 2001, pp. 98-104

Abstract

A three-dimensional model of the 5-HT3 receptor extracellular domain has been derived on the basis of the nicotinic acetylcholine receptor model recently published by Tsigelny et al. Maximum complementarity between the position and characteristics of mutated residues putatively involved in ligand interaction and the pharmacophoric elements derived by the indirect approachapplied on several series of 5-HT3 ligands have been exploited to gain insights into the ligand binding modalities and to speculate on the mechanistic role of the structural components. The analysis of the three-dimensional model allows one to distinguish among amino acids that exert key roles in ligand interactions, subunit architecture, receptor assembly and receptor dynamics. For some of these, alternative roles with respect to the ones hypothesized by experimentalists are assigned. Different binding modalities for agonists and antagonists are highlighted, and residues which probably play a role in the transduction of binding into a change in conformational stateof the receptor are suggested.

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Documento generato il 30/11/20 alle ore 15:44:59