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Titolo:
IDENTIFICATION OF A NEW COMPONENT OF THE AGONIST BINDING-SITE OF THE NICOTINIC ALPHA-7 HOMOOLIGOMERIC RECEPTOR
Autore:
CORRINGER PJ; GALZI JL; EISELE JL; BERTRAND S; CHANGEUX JP; BERTRAND D;
Indirizzi:
INST PASTEUR,CNRS,URA D1284,25 RUE DR ROUX F-75724 PARIS 15 FRANCE INST PASTEUR,CNRS,URA D1284 F-75724 PARIS 15 FRANCE UNIV GENEVA,FAC MED,MED CTR,DEPT PHYSIOL CH-1211 GENEVA 4 SWITZERLAND
Titolo Testata:
The Journal of biological chemistry
fascicolo: 20, volume: 270, anno: 1995,
pagine: 11749 - 11752
SICI:
0021-9258(1995)270:20<11749:IOANCO>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACETYLCHOLINE-RECEPTOR; DELTA-SUBUNIT; LIGAND-BINDING; BUNGAROTOXIN; INTERFACES; CONTRIBUTE; MEMBRANES; RESIDUES;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
P.J. Corringer et al., "IDENTIFICATION OF A NEW COMPONENT OF THE AGONIST BINDING-SITE OF THE NICOTINIC ALPHA-7 HOMOOLIGOMERIC RECEPTOR", The Journal of biological chemistry, 270(20), 1995, pp. 11749-11752

Abstract

Tryptophan 54 of the alpha 7 neuronal nicotinic homooligomeric receptor is homologous to gamma-Trp-55 and delta-Trp-57 of non-alpha subunits of Torpedo receptor labeled by d-tubocurarine. This residue was mutated on the alpha 7-V201-5-hydrorrytryptamine (5HT)(3) homooligomeric chimera, which displays alpha 7 nicotinic pharmacology, and for which both equilibrium binding studies and electro physiological recordings could be carried out in parallel. Replacement of Trp-54 by a Phe, Ala, or His causes a progressive decrease both in binding affinity and in responses (EC(50) or IC50) for acetylcholine, nicotine, and dihydro-beta-erythroidine, without significant modification in alpha-Bgtx binding. Except for Gln-56, comparatively small effects are observed when theother residues of the 52-58 region are mutated into alanine. These data support the participation of Trp-54 to ligand binding, and provide evidence for a new ''complementary component'' of the alpha 7 nicotinic binding site, distinct from its three-loop ''principal component,'' and homologous to the ''non-alpha component'' present on gamma and delta subunits.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 19:14:40