Coupling of ATP Hydrolysis with Channel Gating by Purified, Reconstituted CFTR View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-10

AUTHORS

Christine E. Bear, Canhui Li, Kevin Galley, Yanchun Wang, Elizabeth Garami, Mohabir Ramjeesingh

ABSTRACT

The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride channel situated on the apical membrane of epithelial cells. Our recent studies of purified, reconstituted CFTR revealed that it also functions as an ATPase and that there may be coupling between ATP hydrolysis and channel gating. Both the ATP turnover rate and channel gating are slow, in the range of 0.2 to 1 s(-1), and both activities are suppressed in a disease-causing mutation situated in a putative nucleotide binding motif. Our future studies using purified protein will be directed toward understanding the structural basis and mechanism for coupling between hydrolysis and channel function. More... »

PAGES

465-473

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1022435007193

DOI

http://dx.doi.org/10.1023/a:1022435007193

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1026394396

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9511931


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