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Titolo:
Histidine 186 of the nicotinic acetylcholine receptor alpha subunit requires the presence of the 192-193 disulfide bridge to interact with alpha-bungarotoxin
Autore:
Testai, FD; Venera, GD; Pena, C; Bonino, MJBD;
Indirizzi:
Univ Buenos Aires, Fac Farm & Bioquim, CONICET, Inst Quim & Fisicoquim Biol, RA-1113 Buenos Aires, DF, Argentina Univ Buenos Aires Buenos Aires DF Argentina RA-1113 Aires, DF, Argentina
Titolo Testata:
NEUROCHEMISTRY INTERNATIONAL
fascicolo: 1, volume: 36, anno: 2000,
pagine: 27 - 33
SICI:
0197-0186(200001)36:1<27:H1OTNA>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
BINDING-SITE; RESIDUES; PEPTIDES; TORPEDO;
Keywords:
nicotinic acetylcholine receptor; alpha-bungarotoxin-nicotinic receptor interaction; nicotinic receptor histidine residues; nicotinic receptor structure-function relationship; ligand-gated ionic channels;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Bonino, MJBD Univ Buenos Aires, Fac Farm & Bioquim, CONICET, Inst Quim & Fisicoquim Biol, Junin 956, RA-1113 Buenos Aires, DF, Argentina Univ Buenos Aires Junin 956 Buenos Aires DF Argentina RA-1113
Citazione:
F.D. Testai et al., "Histidine 186 of the nicotinic acetylcholine receptor alpha subunit requires the presence of the 192-193 disulfide bridge to interact with alpha-bungarotoxin", NEUROCHEM I, 36(1), 2000, pp. 27-33

Abstract

We have previously shown that two histidine residues of the nicotinic acetylcholine receptor are relevant for alpha-bungarotoxin binding. This paper studies: (1) the interaction between a-bungarotoxin and the peptide alpha 173-202 - synthesized according to the sequence of the Torpedo californica receptor cr. subunit - and between the toxin and the same peptide containingHis186 modified with ethoxyformic anhydride or substituted by Ala; (2) theinfluence of the presence of Cys192-Cys193 disulfide bridge on such interactions. Solid-phase and in-solution competition assays were performed: ethoxyformylation of His186 or its substitution by Ala led to a significant drop in the toxin binding capacity only for peptides containing the bridge. Circular dichroism and fourth derivate spectra of all peptides were also analyzed. Results strongly indicate the involvement of His186 in the toxin binding to those peptides with the bridge - also present in the native receptor molecules - but not to their reduced forms; on the other hand, they give further support to the already established premise that, though the bridge does not participate directly in receptor-toxin binding, its presence is relevantto define the appropriate conformation of the interaction area. (C) 1999 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 12:47:22