1. Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford University, Stanford, CA 94305, USA;2. Department of Chemistry, Stanford University, Stanford, CA 94305, USA;3. Department of Chemistry and Biochemistry, University of San Diego, San Diego, CA 92110, USA;4. Pasarow Mass Spectrometry Laboratory, NPI-Semel Institute, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA;5. Department of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA;6. SUPA, School of Physics and Astronomy, University of Edinburgh, Edinburgh EH9 3JZ, UK
Abstract:
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Highlights? OADS is a known small-molecule inhibitor of a CLC antiporter ? OADS specifically inhibits the ClC-ec1 antiporter but not the ClC-1 channel ? Photoaffinity labeling and mass spectrometry have localized OADS binding to two discrete sites ? The unique binding mode and lipid dependence of OADS suggest potential mechanisms of action
