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  • The Lectin-like Domain of TNF Increases ENaC Open Probability through a Novel Site at the Interface between the Second Transmembrane and C-terminal Domains of the α-Subunit.

The Lectin-like Domain of TNF Increases ENaC Open Probability through a Novel Site at the Interface between the Second Transmembrane and C-terminal Domains of the α-Subunit.

The Journal of biological chemistry (2016-09-21)
Rudolf Lucas, Qiang Yue, Abdel Alli, Billie Jeanne Duke, Otor Al-Khalili, Tiffany L Thai, Jürg Hamacher, Supriya Sridhar, Iryna Lebedyeva, Huabo Su, Susan Tzotzos, Bernhard Fischer, Armanda Formigao Gameiro, Maria Loose, Trinad Chakraborty, Waheed Shabbir, Mohammed Aufy, Rosa Lemmens-Gruber, Douglas C Eaton, Istvan Czikora
ABSTRACT

Regulation of the epithelial sodium channel (ENaC), which regulates fluid homeostasis and blood pressure, is complex and remains incompletely understood. The TIP peptide, a mimic of the lectin-like domain of TNF, activates ENaC by binding to glycosylated residues in the extracellular loop of ENaC-α, as well as to a hitherto uncharacterized internal site. Molecular docking studies suggested three residues, Val

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Sigma-Aldrich
PR-619, ≥95% (HPLC)