Header

UZH-Logo

Maintenance Infos

The ClC family of chloride channels and transporters


Dutzler, R (2006). The ClC family of chloride channels and transporters. Current Opinion in Structural Biology, 16(4):439-46.

Abstract

The ClC proteins are members of a large family of chloride transport proteins, which are involved in a variety of physiological processes. All family members share a conserved molecular architecture consisting of a complex transmembrane transport domain and a soluble regulatory domain. To date, representative structures for the two parts are available, the transmembrane domain from the structure of a bacterial homologue, the soluble domain from a eukaryotic family member. Despite the strong conservation of the structural framework, the family members show an unusually broad variety of functional behaviors, as some members work as gated chloride channels and others as secondary chloride transporters. The conservation in the structure and the functional resemblance in gating and transport mechanism suggest a strong mechanistic relationship between seemingly contradictory transport modes.

Abstract

The ClC proteins are members of a large family of chloride transport proteins, which are involved in a variety of physiological processes. All family members share a conserved molecular architecture consisting of a complex transmembrane transport domain and a soluble regulatory domain. To date, representative structures for the two parts are available, the transmembrane domain from the structure of a bacterial homologue, the soluble domain from a eukaryotic family member. Despite the strong conservation of the structural framework, the family members show an unusually broad variety of functional behaviors, as some members work as gated chloride channels and others as secondary chloride transporters. The conservation in the structure and the functional resemblance in gating and transport mechanism suggest a strong mechanistic relationship between seemingly contradictory transport modes.

Statistics

Citations

Dimensions.ai Metrics
50 citations in Web of Science®
53 citations in Scopus®
57 citations in Microsoft Academic
Google Scholar™

Altmetrics

Downloads

2 downloads since deposited on 17 Mar 2009
0 downloads since 12 months
Detailed statistics

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:2006
Deposited On:17 Mar 2009 10:52
Last Modified:19 Feb 2018 06:46
Publisher:Elsevier
ISSN:0959-440X
OA Status:Closed
Publisher DOI:https://doi.org/10.1016/j.sbi.2006.06.002
Related URLs:https://biblio.uzh.ch/F/?local_base=UZH01&con_lng=GER&func=find-b&find_code=SYS&request=000194443
PubMed ID:16814540

Download