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Titolo:
IDENTIFICATION OF ACETYLCHOLINE-RECEPTOR CHANNEL-LINING RESIDUES IN THE ENTIRE M2 SEGMENT OF THE ALPHA-SUBUNIT
Autore:
AKABAS MH; KAUFMANN C; ARCHDEACON P; KARLIN A;
Indirizzi:
COLUMBIA UNIV,COLL PHYS & SURG,MOLEC RECOGNIT CTR,630 W 168TH ST NEW YORK NY 10032 COLUMBIA UNIV,COLL PHYS & SURG,DEPT BIOCHEM & MOLEC BIOPHYS NEW YORK NY 10032 COLUMBIA UNIV,COLL PHYS & SURG,DEPT PHYSIOL & CELLULAR BIOPHYS NEW YORK NY 10032 COLUMBIA UNIV,COLL PHYS & SURG,DEPT MED NEW YORK NY 10032 COLUMBIA UNIV,COLL PHYS & SURG,DEPT NEUROL NEW YORK NY 10032
Titolo Testata:
Neuron
fascicolo: 4, volume: 13, anno: 1994,
pagine: 919 - 927
SICI:
0896-6273(1994)13:4<919:IOACRI>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
SITE-DIRECTED MUTAGENESIS; TRANSMEMBRANE PROTEIN-STRUCTURE; NEURONAL NICOTINIC RECEPTOR; AMINO-ACIDS; ION CHANNEL; NONCOMPETITIVE ANTAGONIST; CYSTEINE-SUBSTITUTION; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; SELECTIVITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
M.H. Akabas et al., "IDENTIFICATION OF ACETYLCHOLINE-RECEPTOR CHANNEL-LINING RESIDUES IN THE ENTIRE M2 SEGMENT OF THE ALPHA-SUBUNIT", Neuron, 13(4), 1994, pp. 919-927

Abstract

Each residue in and flanking the M2 membrane-spanning segment of the a subunit, from Glu-241 to Glu-262, was mutated to cysteine, and the mutant subunits were expressed together with wild-type beta, gamma, anddelta subunits in Xenopus oocytes. Cysteines substituted for Glu-262,Leu-258, Val-255, Ser-252, Leu-251, Leu-250, Ser-248, Leu-245, Thr-244, and Glu-241 reacted with the positively charged, hydrophilic, sulfhydryl-specific reagent methanethiosulfonate ethylammonium (MTSEA), added extracellularly. These 10 residues, therefore, are exposed in the channel lumen. The pattern of exposure is compatible with an a helix, interrupted by an extended structure from Leu-250 to Ser-252. Acetylcholine caused subtle changes in the accessibilities of some of the engineered cysteines. Since all 10 residues are accessible to MTSEA in the closed state of the channel, the channel gate is at least as cytoplasmic as Glu-241, the most cytoplasmic of the residues tested.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 16:49:02