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Titolo:
MOLECULAR MODELING OF THE NICOTINIC ACETYLCHOLINE-RECEPTOR TRANSMEMBRANE REGION IN THE OPEN STATE
Autore:
ORTELLS MO; BARRANTES GE; WOOD C; LUNT GG; BARRANTES FJ;
Indirizzi:
UNS,CONICET,INST INVEST BIOQUIM BAHIA BLANCA ARGENTINA UNIV BATH,SCH BIOL & BIOCHEM BATH BA1 7AY AVON ENGLAND
Titolo Testata:
Protein engineering
fascicolo: 5, volume: 10, anno: 1997,
pagine: 511 - 517
SICI:
0269-2139(1997)10:5<511:MMOTNA>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
ION-CHANNEL; NONCOMPETITIVE ANTAGONIST; ALPHA-SUBUNIT; AMINO-ACIDS; MUTATIONS; SEGMENT; DOMAIN;
Keywords:
MOLECULAR MODELING; NICOTINIC ACETYLCHOLINE RECEPTOR; PORE; ION CHANNEL; STRUCTURE-FUNCTION RELATIONSHIPS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
27
Recensione:
Indirizzi per estratti:
Citazione:
M.O. Ortells et al., "MOLECULAR MODELING OF THE NICOTINIC ACETYLCHOLINE-RECEPTOR TRANSMEMBRANE REGION IN THE OPEN STATE", Protein engineering, 10(5), 1997, pp. 511-517

Abstract

A model of the nicotinic acetylcholine receptor transmembrane region has been constructed which may represent the channel in its open-state. The positions of helices flanking the ion channel match those observed by electron microscopy and previously reported by others. Residues labelled, mutated or by other means known to have a strong influence on ion flux are each accessible from the lumen of the modelled channel. The model provides new insights into our current understanding of theion channel structure, and suggests some novel explanations for the results of labelling and mutation studies such as those involving ion channel blockers and residue-dependent changes in ion selectivity.

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Documento generato il 29/09/20 alle ore 07:12:44