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Titolo:
The possible role of a disulphide bond in forming functional Kir2.1 potassium channels
Autore:
Leyland, ML; Dart, C; Spencer, PJ; Sutcliffe, MJ; Stanfield, PR;
Indirizzi:
Univ Leicester, Dept Cell Physiol & Pharmacol, Ion Channel Grp, Leicester LE1 9HN, Leics, England Univ Leicester Leicester Leics England LE1 9HN er LE1 9HN, Leics, England Univ Leicester, Ctr Mechanisms Human Tox, Leicester LE1 9HN, Leics, England Univ Leicester Leicester Leics England LE1 9HN er LE1 9HN, Leics, England Univ Leicester, Dept Biochem, Ion Channel Grp, Leicester LE1 7RH, Leics, England Univ Leicester Leicester Leics England LE1 7RH er LE1 7RH, Leics, England Univ Leicester, Dept Chem, Ion Channel Grp, Leicester LE1 7RH, Leics, England Univ Leicester Leicester Leics England LE1 7RH er LE1 7RH, Leics, England
Titolo Testata:
PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY
fascicolo: 6, volume: 438, anno: 1999,
pagine: 778 - 781
SICI:
0031-6768(199911)438:6<778:TPROAD>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
SELECTIVITY FILTER;
Keywords:
channel assembly; disulphide bond; potassium channel;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
8
Recensione:
Indirizzi per estratti:
Indirizzo: Stanfield, PR Univ Leicester, Dept Cell Physiol & Pharmacol, Ion Channel Grp, POB 138, Leicester LE1 9HN, Leics, England Univ Leicester POB 138 Leicester Leics England LE1 9HN gland
Citazione:
M.L. Leyland et al., "The possible role of a disulphide bond in forming functional Kir2.1 potassium channels", PFLUG ARCH, 438(6), 1999, pp. 778-781

Abstract

The role of two cysteine residues - Cys122 and Cys154 - in the structure of the strong inward rectifier K+ channel, Kir2.1, has been investigated using site-directed mutagenesis and electrophysiology. Such cysteine residues are conserved across the inward rectifier family and may be expected to form a crucial disulphide bond. Our experiments show that when the cysteines are absent, the protein is expressed, but the channels are not functional, suggesting that the disulphide bond is essential for correct channel assembly. However, reducing agents applied extracellularly have little effect on current amplitude in wild-type, so that, once the channel is assembled correctly in the membrane, the disulphide bonds are no longer essential for function. Molecular modelling suggests that a disulphide bond is formed - this may be either an intra- or an inter-subunit.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 09:44:42