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News Physiol Sci 15: 154-158, 2000;
1548-9213/00 $5.00
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News in Physiological Sciences, Vol. 15, No. 3, 154-158, June 2000
© 2000 Int. Union Physiol. Sci./Am. Physiol. Soc.

Stimulatory and Inhibitory Functions of the R Domain on CFTR Chloride Channel

Jianjie Ma

J. Ma is an Associate Professor in the Department of Physiology and Biophysics at Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106.
CFTR is a chloride channel whose gating process involves coordinated interactions among the regulatory (R) domain and the nucleotide-binding folds (NBFs). Protein kinase A phosphorylation of serine residues renders the R domain from inhibitory to stimulatory and enables ATP binding and hydrolysis at the NBFs, which in turn control opening and closing of the chloride channel.




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