Key result
Deletion or mutation of residues 278-283 in the extracellular loop of the alpha-subunit of ENaC altered amiloride binding affinity and reduced mean open times compared to wild-type channels.
Population
Epithelial sodium channels (ENaC) formed from wild-type or mutant alpha-subunits
Comparison
Mutations in the extracellular loop of the… vs Wild-type alpha-subunits
Design
Preclinical
Authors
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May guide ENaC drug design; extends structural insights but leaves open human translation.
The extracellular loop of the ENaC alpha-subunit (residues 278-283) plays a critical role in amiloride binding and channel gating.
Kelly et al. (2003) studied this question. Mutations in residues 278-283 of the alpha-subunit of ENaC vs. Wild-type alpha-subunits was evaluated on Amiloride binding affinity and channel gating. Deletion or mutation of residues 278-283 in the extracellular loop of the alpha-subunit of ENaC altered amiloride binding affinity and reduced mean open times compared to wild-type channels.
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