Journal article
Block by MOPS reveals a conformation change in the CFTR pore produced by ATP hydrolysis
American Journal of Physiology: Cell Physiology, Vol.273(4), pp.C1278-C1289
10/01/1997
DOI: 10.1152/ajpcell.1997.273.4.C1278
PMID: 9357772
Abstract
ATP hydrolysis by the cystic fibrosis transmembrane conductance regulator (CFTR) Cl− channel predicts that energy from hydrolysis might cause asymmetric transitions in the gating cycle. We found that 3-( N-morpholino)propanesulfonic acid (MOPS) blocked the open channel by binding to a site 50% of the way through the electrical field. Block by MOPS revealed two distinct states, O1 and O2, which showed a strong asymmetry during bursts of activity; the first opening in a burst was in the O1 state and the last was in the O2 state. Addition of a nonhydrolyzable nucleoside triphosphate prevented the transition to the O2 state and prolonged the O1 state. These data indicate that ATP hydrolysis by the nucleotide-binding domains drives a series of asymmetric transitions in the gating cycle. They also indicate that ATP hydrolysis changes the conformation of the pore, thereby altering MOPS binding.
Details
- Title: Subtitle
- Block by MOPS reveals a conformation change in the CFTR pore produced by ATP hydrolysis
- Creators
- Hiroshi Ishihara - Howard Hughes Medical Institute, Departments of Internal Medicine and Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Michael J Welsh - Howard Hughes Medical Institute, Departments of Internal Medicine and Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242
- Resource Type
- Journal article
- Publication Details
- American Journal of Physiology: Cell Physiology, Vol.273(4), pp.C1278-C1289
- DOI
- 10.1152/ajpcell.1997.273.4.C1278
- PMID
- 9357772
- ISSN
- 0363-6143
- eISSN
- 1522-1563
- Language
- English
- Date published
- 10/01/1997
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Pulmonary, Critical Care, and Occupational Medicine; Neurosurgery; Internal Medicine
- Record Identifier
- 9984020996002771
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