The possible role of a disulphide bond in forming functional Kir2.1 potassium channels

M. L. Leyland, C. Dart, P. J. Spencer, M. J. Sutcliffe, P. R. Stanfield

    Research output: Contribution to journalArticlepeer-review

    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 cystein 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.
    Original languageEnglish
    Pages (from-to)778-781
    Number of pages3
    JournalPflügers Archiv European Journal of Physiology
    Volume438
    Issue number6
    DOIs
    Publication statusPublished - 1999

    Keywords

    • Channel assembly
    • Disulphide bond
    • Potassium channel

    Fingerprint

    Dive into the research topics of 'The possible role of a disulphide bond in forming functional Kir2.1 potassium channels'. Together they form a unique fingerprint.

    Cite this