Format

Send to

Choose Destination
See comment in PubMed Commons below
Nature. 1996 Sep 26;383(6598):337-40.

Homodimeric architecture of a ClC-type chloride ion channel.

Author information

1
Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254, USA.

Abstract

The recent discovery of the ClC-family of anion-conducting channel proteins has led to an appreciation of the central roles played by chloride ion channels in cellular functions, such as electrical behaviour of muscle and nerve and epithelial solute transport. Little is known, however, about molecular architecture or sequence-function relationships in these membrane proteins. In the single case of ClC-0, a voltage-gated 'muscle-type' chloride channel, the functional complex is known to be a homo-oligomer of a polypeptide of Mr approximately 90,000, with no associated 'helper' subunits. The subunit stoichiometry of ClC-type channels is controversial, however, with either dimeric or tetrameric association suggested by different indirect experiments. Before a coherent molecular view of this new class of ion channels can emerge, the fundamental question of subunit composition must first be settled. We have examined hybrid ClC-0 channels constructed from functionally tagged subunits, and report here that ClC-0 is a homodimer containing two chloride-conduction pores.

PMID:
8848046
DOI:
10.1038/383337a0
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Nature Publishing Group
    Loading ...
    Support Center