Coupling of ATP hydrolysis with channel gating by purified, reconstituted CFTR

Autor:	C E, Bear, C, Li, K, Galley, Y, Wang, E, Garami, M, Ramjeesingh
Rok vydání:	1998
Předmět:	Adenosine Triphosphate Hydrolysis Cystic Fibrosis Transmembrane Conductance Regulator Humans Ion Channel Gating Models Biological
Zdroj:	Journal of bioenergetics and biomembranes. 29(5)
ISSN:	0145-479X
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::318d68797242b3f812d16a21e3de8789 https://pubmed.ncbi.nlm.nih.gov/9511931 Zobrazit plný text záznamu Full text from SpringerLink