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Titolo:
AMINO-ACID-RESIDUES LINING THE CHLORIDE CHANNEL OF THE CYSTIC-FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR
Autore:
AKABAS MH; KAUFMANN C; COOK TA; ARCHDEACON P;
Indirizzi:
COLUMBIA UNIV,CTR MOLEC RECOGNIT,630 W 168TH ST NEW YORK NY 10032 COLUMBIA UNIV,DEPT PHYSIOL & CELLULAR BIOPHYS NEW YORK NY 10032 COLUMBIA UNIV,DEPT MED NEW YORK NY 10032
Titolo Testata:
The Journal of biological chemistry
fascicolo: 21, volume: 269, anno: 1994,
pagine: 14865 - 14868
SICI:
0021-9258(1994)269:21<14865:ALTCCO>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
SITE-DIRECTED MUTAGENESIS; XENOPUS OOCYTES; CYSTEINE-SUBSTITUTION; MILD-DISEASE; CL CHANNELS; CFTR GENE; R-DOMAIN; RECEPTOR; SELECTIVITY; MUTATIONS;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
M.H. Akabas et al., "AMINO-ACID-RESIDUES LINING THE CHLORIDE CHANNEL OF THE CYSTIC-FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR", The Journal of biological chemistry, 269(21), 1994, pp. 14865-14868

Abstract

The cystic fibrosis transmembrane conductance regulator forms a chloride channel that is regulated by phosphorylation and intracellular ATPlevels. The structure of the channel-forming domains is undetermined. To identify the residues lining this channel we substituted cysteine,one at a time, for 9 consecutive residues (91-99) in the M1 membrane spanning segment. The cysteine substitution mutants were expressed in Xenopus oocytes. We determined the accessibility of the engineered cysteine to charged, sulfhydryl-specific methanethiosulfonate reagents added extracellularly. We assume that, among residues in membrane-spanning segments, only those lining the channel will be accessible to reactwith these hydrophilic reagents and that such a reaction would irreversibly alter conduction through the channel. Only the cysteines substituted for Gly-91, Lys-95, and Gln-98 were accessible to the reagents. We conclude that these residues are in the channel lining. The periodicity of these residues is consistent with an alpha-helical secondary structure.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 20:41:03