Format

Send to

Choose Destination
See comment in PubMed Commons below
Arch Biochem Biophys. 2008 Aug 1;476(1):95-100. doi: 10.1016/j.abb.2008.03.033. Epub 2008 Apr 8.

Molecular basis for the ATPase activity of CFTR.

Author information

1
Programme in Molecular Structure & Function, Research Institute, Hospital for Sick Children, 555 University Avenue, Toronto, Ont., Canada.

Abstract

CFTR is a member of the ABC (ATP binding cassette) superfamily of transporters. It is a multidomain membrane protein, which utilizes ATP to regulate the flux of its substrate through the membrane. CFTR is distinct in that it functions as a channel and it possesses a unique regulatory R domain. There has been significant progress in understanding the molecular basis for CFTR activity as an ATPase. The dimeric complex of NBD structures seen in prokaryotic ABC transporters, together with the structure of an isolated CF-NBD1, provide a unifying molecular template to model the structural basis for the ATPase activity of CFTR. The dynamic nature of the interaction between the NBDs and the R domain has been revealed in NMR studies. On the other hand, understanding the mechanisms mediating the transmission of information from the cytosolic domains to the membrane and the channel gate of CFTR remains a central challenge.

PMID:
18417076
DOI:
10.1016/j.abb.2008.03.033
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center